Biochemistry and Metabolism
What happens to the nutrients any organisms take in? name one way? how do they become part of the body? what are they used to provide?whats that energy needed for? what is metabolism? define: metabolism? what happens to substances that cant be digested? what are organims adapted for? give one example? what does fibre help remove? what is a diet low in fibre? define: risk factor?
What organisms made up of? in order to survive what must an organism be able to do? what do these molecules fall into? what does each chemical group have? name the 6 different groups? and theyre role? what is fibre a type of?
What are the key biological molecules?What is the structure of each biological molecule related to? what are the chemical elements found in biological molecules? what percent do these elements make up organisms? what do a few molecules aso contain a little of? what three minerals can be considered seperatly? what percent of a cel is water? what percent is chemials? what is the bulk of the chemcials? what are the other five?
What can matabolic reactions involve? what are these reactions called? give example? what is the other type of reaction called? what does it involve? give example?
what does all the biological molecules have in commonm? except which one? what cna carbon atoms bond togther to form? what is then possible? to form what? what will these have? due to this mutiple bonding feature what is carbon like?
build and maintain a healthy body, they become part of your body, after being broken down intosmaller pieces (digested) they are rebuilt to form the different parts of the organism, the energy needed to drive metabolism, living processes, is the sumtotal of all the biochemical reations taking place in the cells of an organism, removed from the body, remove these substances in a variety of ways, human intestine works best when indegistable fibre is present in food, waste products like excess bile salts which can be toxic, is a risk factor for a number of diseases like cancers,
thousands of different molecules, make or take in all the molecules required, chemical groups, differing roles in the organism, carbohydrates- energy sotrage and supply and structure, Proteins- structure transports enzymes antibodies hormones, Lipids- membranes energy supply hermal insulation protective layers electrical insulation in neurosn enzyme activators, Nucleic Acids- information molecules carry instructions for life, Water- in reactions, support in plants, solvent for most metabolic reactions transport, carbohydrate,
Carbohydrates lipids proteins and nucelic acids, function withing living organisms, carbon hydrogen oxygen and nitrogen, 99%, phosporuse and sulfur, magnesium iron and iodine, 70%, 30%, proteins, Rna ions small molecules polysacchardies phospholipuids and DNA,
breaking larger molecules into smaller ones, catabolic reactions, digestion, building smaller molecules into larger ones called anabolic, muscle growth,
carbon-based, water, long chains and rings, bond other atoms to the chains and rings to form many diffferent molecules, structure and properties, framework atom that can form the basis of al the biological molecules meccassary for life
Biochemicals and Bonds
When are atoms most stable? what is this number usually? how may electrons in carbon's outer orbitals? how many do they need for stabiity then? with what? what does the sharing of electrons form? between what? whats this bond known as? define: covalent bond? what do the bonded atoms form? is a molecule stable? why?
what does carbon form in some cases? where are C=C double bonds found? where are C=O double bonds found?
how are biological molecules grouped? how are large molecules made? what does the term monomer refer to? what happen to them? to form what? why are lipids not polymers? give the biological molecule and name its monomer and polymer?
What is the chemical reaction that lins biological monomers together caled? what happens to make a polymer? what do condnsation reactions also link? What happens first in a condensation reaction? what bond is formed? what is formed? how? what is the chemical reaction that splits larger molecues to monomers aclleD? what is hydrolysis? In a hydrolysis reaction what happens first? what is bond is broken what is formed?
What size can polymers be? what do they often have? what does this rely on? when do hydrogen bonds form? when is this easily seen? describe hydrogen bonds? how many can be found in polymers? what do they help?
outer energy levels contain a specific number of electrons, 8, 4, 4, with the same or other atoms, strong bond between the atoms, covalent bonds, formed when electrons are shared between atoms and are very strong and covaently bonded atoms form new molecules, molecule, very stable, because each atom in the molecule is sharing the electrons to give a stable full outer energy level,
two bonds with another atom, hydrocarbon chains, many molecules,
chemical properties, large molecules are made by bonding together similiar smaller molecules, refers to single small molecules, polymer, because the smaller molecules are very differnet from each other, carbohydrtaes- monosacchardies and polysaccahrides, proteins- amino acids and polypeptides & protiens, Nucleic Acids- Nucleotides and DNA & RNA
condensation reaction, the same reaction is repeated many time in order to link many monomers together to forma polymer, link different subunits together in lipid molecules, a wtaer molecules is released, a covalent bond is formed and a large moelcules is formed by the bodning of smaller molecules, hydrolysis reaction, reverse of condensation, a water molecule is used, a covalent bond is broken and a smaller molecule is formed by the splitting of a large molecule
Very large molecules, specific functions, shape, whena slightly negatively charged part of a molcule comes to a slightly positive charged hydrogen atom in the same or another molecule, water, weak bonds, many thousands of hydrogen bonds can form and this heps stablise the structure of the molecule
Carbohydrates 1: Simple Sugars
What percent does carbohydrates make up the organic matter of a cll? What are the three functions of carbohydrates in organisms? wheres the energy come from? example of storage? examle of structure? what do some carbohydrates form part of? example? what elements do carbohydrates contain? why does carbohydrate essentailly mean hydrated carbon? what does this mean?
Define Carbohydrate?Whart are the simpliest carbohydrates called? what are these? how are larger carbohydrates made? are there more than one monosaccahride? how many carbon atoms can they contain? what are the three similiar properties? How are the monosaccharides grouped? what is 3-carbon monosacharides called? 5-carbon monosacharides called? and 6-carbon? what are the most common? what do these include? how many water to carbon? write the formula? what do pentose and hexoses tend to occur in nature as?
How can glucose be drawn? In the ring structure how comes it can be drawn in 2 slightly different ways? What is it called if the OH at Carbon1 is below the plane? and what if it is above? what does this difference in structure lead to? Draw the chain and ring form of alpha and beta glucose? what are differnt shaped forms of the same molecule called?
What can be joined together? in what reaction? what two things does this form? give example? a new what bond is formed? called a what ond? what is eliminated? what is the reverse? how doies it break the glycosidic bond? name three pollysachardes? give example of breaking down larger molecules? what do all of these involve? are disacchardides still sugars?
10%, energy source energy store structure, released from glucose during respiration strach cellulose, form parts of larger molecules, nucleic acids glycolipids, carbon hydrogen oxygen, because the elements are found in the proportions Cn(H2O)n, meaning for every carbon present in a carbohydrate a water molecule is presnt
Carbohydratess make a group of molecules containg carbon hydrigen and oxygen in the ratio Cn(H2o)n, monosaccharides, monomers, joining monosaccharides togeter, a nuber of different monossachharides, between 3 and 6, soluable in water are sweet tasting and form crystals, to the number of carbon atoms in the molecule, triose sugars, pentose sugars, hexose sugars, hexoses, glucose and fructose, 1:1, C6H12O6, in nature as rings
cahin or ring structure, as the H and OH at Carbon 1 may be obove or beliw the plane of the ring, Alpha glucose, Beta Glucose, different properties, isomers
Two monosacchardies, condensation, a dissachride molecule and water, covalent bond, glycosiidic bond, water, hydrolysis reaction, uses a water moleule to break the glycosidic bond, starch glycogen cellulose, digestion, involve the making and breaing of glycosidic bonds, are still suagrs,
Carbohydrates 2: Energy Storage
What do glucose molecules contain a large number of? what can happen to them? whats broken into what during what to release energy? what can this energy be used to make? give respiration equation? what is each step of the breaking down of glucose driven by? to use the glucose in respiration what does an organism need? do animals and plants have enymes to break down alpha and beta glucose? why cant it break beta glucose? can both alpha and beta glucose be respired?
What do two alpha glucose molecules bonded together form? called what? so how is the molecue amylose formed? What can amylose consist of? where does the glycosidic bond between all the glucose subunits occcur? so whats it caled? what shape does the long chain of amylose make? why? what does this make amylose quite? what molecules can become trapped in the molecules? whats the difference between the large molecules and the lucose molesu from which they are formed?
What is starch? what two things does starch consist of? what is starch in plants a mixture of? what two places is it stored? where are there a lot of strach grains? what can starch be broken down to? which can then be?
What is glycogen? what is glycogen sometimes referred to as? how is it identicla to starch? whats different about the glucose chains in glyogen? what does this mean? what does it form? where?
Why are strach and glycogen described as energy-storage molecules? what dont starch and glycogen both not do? what does this mean? why is this feature vital? whats the signifcane of holding glucose in chains?
Number of bonds thatt can be broken to form simpe molecules, glucose into simplied molecules of water and carbon dioxide in respiration releases energy, ATP, glucose + oxygen->carbon dioxide + water + energy that is used to form ATP, enzyme, must have enzymes that can specifically break the glucose molecule, only alpha glucose, because of its differetn arrangment of the H and OH at C1 this is because enzyme function is based on shape, only alpha glucose
disaccharide called maltose, the same condensaton reaction can be carried out over and over again to join gucose molecules together, many thousands pf glucosemolecules bonded together, carbon number 1 of one molecule and carbon number 4 of the next, 1,4-glycosidic bond, coil into a spring, because of the shape of the glucose molecues and the formation of the glycosidic bonds, compact, iodine molecules, they are not water soluable
the energy storage polysacharride in plants, mixture of long straight chains amylose molecules and branched amylopectin, amylose and amylopectin, chloroplasts and in the plant cell in membrane-bound starch grains, cell plant storage organs lie potatoa tubers, to glucose molecules which may then be respired to release energy
the energy-storage polysaccharide in animals, animal strach, its made up of alpha gluvose subunits and it s alarge molecule that can be broken down to release the glucose to be respired, the 1,4 linked glucose chains are shorter and have more branches, more compact, glycogen granules, live and muscle cells
because both starch and glycogen are made by bonding thousand of alpha glucose molecules togetehr, they dont dissolve, stored glucose doesnt afect the water potential of the cell, as glucose sotred in a cell as free molecules would dissolve and reduce water potential, so they can be easily broken off from the ends to provide glucose for respiration when required
Carbohydrates 3:Structural Units
Beta glucose molecules can be bonded together in a what? called? how does it happen? what can alpha gluvose molecules be ondensed to form? are beta glucose the same as alpha when they condense? why? what are they like? what happens to the second beta glucose molecule? how many b glucose molecules in these straight chains? are they stronger or weaker than the chains in amylose? what are these beta glucose poymer chains called? where is cellulose found?
How are cellulose fibres arranged? what do they form? why can many hydrogen bonds form between the glucose monomers? how many cellulose molecules become cross linked by hydrogen bonds? what do they form? what are these held by? to form what? called what? what do the macrofibrils have great of? where are they embedded? to form what?
where are cell walls? what does it give each cell? which supports what? what does the arrangemnet of macrofibrils allow? why doesnt water moving into plant cells cause it to burst? what if it becomes turgid? what does the arrangemtn of macrofibrils in cell walls determine? what can cels walls be reinforced with to do what? or what?define: cellulose?
Name two other organisms that use structural carbohydrate poymers? how?
Name a carbohydrate monomer? give 2 examples? how many carbons in each? characteristics? role in organism? Name a carbohydrate dimer? example and what its made from? charcteristics? role in organisms? name carbohyrdtae polymer? give 3 examples? characterisitics? role in organisms?
in a long chain, polymer, through numerous condensation reactions, coiled spring like chains, no, due to their slightly differnt shape the resulting chains are long and straight, rotated 180degrees, 10,000, stronger, cellulose chains, only in plants,
in a very specific way, plant cell walls, because theglucose monomers conain so many OH groups, 60-70, bundles called microfibrils, together by more hydrogen bonds to form larger byundles called macrofibrils, mechanical strength, polysachharide glue of substances called pectins, the cell wall
around the plant cells, great strength, supporting the whole plant, allows water to move through andd along cells and in and out of the cell easily, the wall prevents the bursting and if its turgid it helps to support the whole plant, how cells ca gror or change shape, other substances to provide extra support or to make the walls waterproof,is a carbohyrdtae polymer made by bonding beta glucose molecule together in long chains,
insects exoskelton is formed from the polysachharide chitin and cell walls found around bacteria cell is formed from the polysachcharide peptidoglycan
Monosaccharide, Glucose 6 carbon provides enerfy via respiration and deoxyribose 5 carbon part of DNA, smallsoluabe sweet crystaline, disaccharide, maltose made from two glucose molecules, small soluabe sweet crystaline, sugar obtained when starch is broken down in hydrolysis reaction and can be split furhter to gain glucose for respiration, polysaccharide, starch and glycogen which are made of large alpha molecules joined by condensation reaction insoluable in waer forms grains its an energy storage carbohydrates,, cellulose made from large beta glucose molecules joined by condensation reactions insolubale and stron, job is structural in plants to form cell walls
Amino Acids- Monomers of proteins
What percent does proteins make up organic mater of a cell? small or large molecules? whats elements make it up? what can some proteins contain? Protein Functions- give one function? example? what do they do for membranes? examples? all _____ are protiens? many ____ are proteins? _____ are proteins? overall what do proteins provide? what activity are they crucial for?
why are protiens large molecules? how are they made? what are the monomers called? what does a protein consist of then?
what do all amino acids have? what do they have at one end of the molecule? what elemtns make this up? at the other ther? what elements make this up? and what inbetween? what do amino acids joined end-to-end give a repeating? are all amino acids identical? how many types of naturally occuring amino acid? why are there differences? what is the r group in glycine? can the r group be larger tgab the C-C-N part of the molecule? what charge are they? are they hydrohphibc or hydrophilic?draw basic structure of amino acid?
What are plant able to do? provided what? what is the nitrate converted to? and bonded to? made from? How do animals get protein? what happens to these proteins? what can then be built? can aniamls get all the amino acids they need from ,aterials? how many cant? what are these called? where are they found? do plants contain more or fewer? what type of person needs to be careful because of this?what contains all of them? define: amino acids?
What happens if the amino acids are sirplus to the body requirments? why? what happens to it? whats the process called? where in mammls does this process take place? what are the amino groups removed converted to? how is it removed?
50%, large molecules, carbon hydrogen oxygen and nitrogen,sulfur, structurla components e.g. of muscle and bone, membrane carriers and pores e.g. for active transport and facillitated difusion, enzymes, hormones, antibodies, building materials important for growth and reapir, metabolic activity,
because they are polymers, joining together a large number of similiar smaller subunts (monomers) amino acids, of a ong chain of amino acids joined end to end,
Same basic structure, amino group, Nitrogen bonded to hydrogen atoms, acid group, carbon double bonded to oxygen and an OH group, carbon bonded to hydrogen atom and the R-group, backbone, N-C-C-N-C-C-N-C-C, no, 20 types, they have different R-groups, hydrogen atom, can be larger, positve or negative, hydrophilic or hydrophobic,
able to manufacture the amino acids they need, they can obtain nitrate from soil, amino groups and bonded to organic groups made from products of photosynthesis, take in protein from diet, digested into amino acid, proteins,no, 8-10, essential amino acids, meat, fewer, vegetarians, soya
cannot be stored, the amino group makes them toxic if to much is present, removed in deamination, liver, urea, removed in the urine
Joining amino acids together
does the r-group affect the way the amino acid is joined? what reaction has to happen? between what parts of the amino acids? what bond is formed? what is also produced? what is the new bond formed called? what is the molecule produced called? how is the peptide bond broken? what does it use? when is the making and breaking of peptide bonds required?
no they are joined the same way, condensation reaction, the acid group f one amino acid and the amino group of another, covalent bond, water molecule, peptide bond, dipeptide, hydrolysis reaction, uses a water molecule to break the bond, is required in the buiding and rebuilding of all protein molecues in organisms and in breaking down proteins to amino acids for example in digestion
Proteins from Amino Acids
What do to two amino acids joined form? what is formed as more and more are joined together? by what bonds? whats the minimum amount of polypeptide chains? how many amino acids in this? how many in larger protiens? what are amino acids in polypeptide chains sometimes referred to as amino acids residues? why?
Where are polypeptides and proteins synthesised? what does synthesisied mean? what is this process known as? what happens here? what doe it use to do this? to make what? what happens as the mRNA passes through the ribosome? what occurs as each new amino acids joins? what bond is formed? whats produced? what is the sequence determined by? how do you make a different protein?
How many proteins may an oorganism contain? what does each protein have? what is each on formed from? joined by what? in a what? how many amino acids in a protein? what does each one have though? what is the function of each one determine by? what is the structure firstly determined by? what is this unique amino acid sequence? define: primary structure? what do different amino acids have? what will the amino acids sequence effect the protein? give example?
calculation for the possibile sequence of amino acids with if there are four amino acids in the peptide chain?
what catalyzes the formation and breakin of peptide bonds and every other type of covalent bond? are covalent bonds strong or weak? can the natural conditons of a cell make or break then? what enzymes that catlyse the make or break of peptide bonds? where are they found? give one example? why do hormones need to be broken down? what does a cell targetted by a hormone contain? why? give another example? whats a feature of ageing? why does this occur?
Dipeptide, polypeptide, peptide, single polypeptide chain, hundreds of amino acids, more than one polypeptide chain, amino acid residue, because part is lost in the condensation bond,
In cells on ribosomes, where they are made, protein synthesis, amino acids are put in the right order, information molecule called messenger RNA (mRNA), to make a specific polypeptide chain, amino acids are joined together one at a time, condensation reaction, peptide bond, longer and longer chain of amino acids, the mRNA, different mRNA molecule must passs through ribosome
10,000, own function, amino acids joined by a polypeptide bond in a chain, hundreds, one amino group and one acid group, structure, amino acid sequence, primary structure, primary structure of a protein is given by the specific sequence of amino acids that make up the protein, properties, effect on its properties, if the protein contains a number of amino acids with hydrophibic R-gorup then the final protein will be a particuar shape and may be found embedded in the a membrane
20x20x20x20= 160,000 because the amount of amino aicds in the chain x the amount of differnet types of amino acids possible i.e. 20
enzymes, strong, no, protease enzymes, where organisms continually break down and rebild proteins (majoirty of places in the organism) hormone regulation, that their effects are not permenant and can be controlled, enzymes tat can break down that hormone, Ageing, skin loses elasticity and becomes wrinkled, old skin is less able t rebuild the protein collagen and other proteins that give young skin its smooth and elastic properties
Levels of protein structure
To make a specific protien _____ must be bonded in a _____ _____? What is this sequence determined by? as more amino acids are bonded what does the chain become? how is tangling and breaking avoided? what bonds hold these coils and pleates? what does the amount of coiling or pleating depend on? and so depends on what structure? what is formed when the chain is completed? what happens to the coils and pleats now? to form what? what is the overall shape determined by? what are the levels of protein structure
What is the primary structure?
When is the secondary structure formed? to form what? or? what holds the coils in place? describe the strength of hydrogen bonds? how many? what do they giver overall? Define:secondary structure? hw many amino acids in alpha helix per 10 turns of the coil? where do the hydrogen bonds form?
When is the final three dimensiona shape of a protein formed? whats often inbetween? what is this three dimensional shape held in place by? what is a proteins tertiary structure vital to? give example? Give a structural protein? whats it shaped to be? how? what must an enzyme have? whats this complementary to? Define: teritary structure?
what bonds stabalise the tertiary structure?What does the amino acid cysteine contain? what is formed when two cysteines are close to each other? What do r-Groups sometimes carry? positive or negative? whats found when oppositly charged amino are close to each other? whats bond if dounf where oppsitly charged groups are found near each other? in a water based enviroment when aree hydrophobic amino acids moist stabke? where aer hydrophilic amino acids often found? in what? with what in the centre?
amin acids specific sequence, DNA, longer and longer, stabalised by being colied up or pleated as they are made, numerous hydrogen bonds, on the type of amino acids being added to the chain, primary structure, polypeptide, the coils and pleats come together in a specific wayy to form a specific overall 3d shape, orgianly sequence of amino acids (R-groups in the primary structure), primary secondary tertiaryand in some cases quaternerary
This is the sequence of amino acids that forms the protein
when the chain of amino acid coils or folds to form an alpha helix or a beta pleated sheet, hydrogen bonds, quite weak, many are formed, give great stability to parts o the protein olecule, refers to coiling and pleating of parts of the polypeptide molecule, 36, one amino acid and teh one "four places" aong the chain
when these coils and pleats themselves coil or fold. straight runs of amino acids, a number of diffferent types of bonds and interaction (disfulide ionoic and hydrogen bonds and hydrophobic and hydrophilic interactions), function, hormone must be a specific shape in order to fit into the hormone receptor of a target cell, collagen is shaped to be strong with protein chains would around each other in a specfici way, active sit the sape which is complementary to that of its substrate
disfulide ionic and hydrogen bonds and hydrophic and hydrophilic interactions, sulfur, a covalent bond called disulfide bond is formed, charge either positive or negative, ionic bond forms, hydrogen bonds forms, if water is excluded, outisde of globular proteins, hydrophobic amino acids,
Levels of protein structure
What does heating a protein increase? what does this cause the molecule to do? what breaks? why are most of the bonds holding the tertiary structure weak? are they easily broken? What happens if enough heat is applied? what will it no longer do? whats this process called? what is the protein said to be? what if the protien is then cooed?
what do the three dimensional shape of proteins fall into? what are they? what do globular tend to do? what happens to the hydrophobic R-groups? whats its usual role? give two examples and where they are found? while the hydrophilic? what does this make the protein? why? what do fibrous proteins form? what do most have? what are they in water? give two examples and where its found?
kinetic energy in the molecule, causes it to vibrate, breaks the bond holding the teriary structure in place, they are not covalent bonds, they are easily broken, the whole tertiary structure can unravel and the protein will no longer function, denaturation, denatured, it will not reform the origina complex structure
fall into two main categories, globular and fibrous, roll up into a compact globe or ball structure, are turned inwards toward the centre of the structure, tend to be outside, this makes the proteins water-soluable because water molecules can easily cluster around them, metabolic roles, enzymes found in all organisms and plasma protiens and antibodies found in mammals blood, form fibres, regular repeitive sequences of amino acids, insooluable in water, structural roles, collagen in bone and cartilage and keratin found in fingernails and hair
Proteins in Action
What does the quaternary structur refer to? or? when do such proteins only function? what may the quaternerary structure involve? or? give two examples of proteins with a quaternary structure?
How many polypeptide subunits does haemoglobins quaternary structure consist of? what are 2? what are the other 2? the four together form what? is water soluable or not? is it globular or fibrous? as with all proteins what holds the teriatry strcture in place what do these interactions give the subunits and hence the complete molecule? what is the shape vital for? what is haemoglobins function? what does it bind? and releases it where? what is a specialised part of each polypeptide called? what does it contain? what is this responsible for in haemoglobin? give equation? what can bind to the iron in te haem group? how mnay oxygen can bind to haemoglobin then? is the haem group made of amino acids? what are they called? define: haemoglobiin?
What type of protein is collagen? how many polypeptide chains does it have?what does it look like? what is each of the three chains as itself? made up of how many amino acids? what forms between the chains? what does this give? how is the strength of the molecule increased further? what are these called? what adds to the strength? what is the result? what do many fibrils together form? what is the function of collagen? what walls is collagen found? what does the layer prevent? what are tendons mostly? what do they connet? what does the collgaen allow? what are bones formed from? reinforced with what? to make them what? what are cartilage and connetcive tissue made from? why are cosmetic treatments using treatment becoming increasingly popular? define: collagen?
Haemoglobin and collagen comparison- what is globular? whats the other? whats insoluable in water? whats the other? differnece in amino acids? which contains prosthetic group? what sort of helix structure does each have?
to the fact that some proteins are made up of more than one polypeptide subunit joined together, a polypeptide and an inorganic component, if all the subunits are present, two identical polypepitides coming togtehr to form the final working protein, a number of different polypeptude subunits coming together, haemoglobin and insulin,
four, apha chains, beta chains, haemoglobin molecule, water soluable, globular, number of differens bonds and interactions, a very specific shape, carry out its function, oxygen from the lungs to tissues, in the lungs, tissues, haem group, iron ion, the colour, haemoglbin (purple-red)+oxgen00. oxyheabolgin(bright red), oxygen, four, not made from amino acids, prothetic groups, is a globular transport protein
fibirous, three wound around each other, twisted rope, is a coil, 1000amino acids, hydrogen bonds, the structure strength, each collagen molecule forms covalent bonds with other collagen molecules next to it, cross-links, staggered along the collagen molecules, collagen fibril, collagen fibre, mechanical strength in many areas, walls of arteries, prevents blood being pumped from the heart at high pressure bursting the walls, collagen, connect skeltal muscles to the bone, form a strong connection that allows muscles to pull bones for movement, collagen, materials such as calcium phosphate, to make them hard, collagen, it can be injetced into lips to give them fuller appearance, is a fibrious structural protein
haemoglobin is globular, collagen is fibrous, haem is soluable in water, coll is insoluabe, heam has a wide range of amino acid constitunets in primary structure, coll- approx 35% of the molecules primary structure is one type of amino acid (glycine), haem contains a prosthetic, haem- much i wound into alpha helix structurees, col- much consist of left handed heix structures
Lipids are not Polymers
What percent do lipids make up the organic matter of a cell? at room temp what is a solid lipid called? and a liquid one is called? Lipids functions- can lipids be respired? to realse what? to generate what? whats there function then? what are they also for energy? where are lipids stoored?/ what are they? what are all biological membranes made from? what is whales blubber made from? what function is this? what other insulation do they provide? what do plants leaves hae a layer of? to do what? what function is this? what are some hormones? example? what elements do lipids contain? is oxygen low or high? much lower in comapiroson to what other biological molecule? are they soluable or insolubale in water? define: lipid? draw glycerol?
where are glycerol and fatty acids are found in all fats and oils that perform roles where? and are also found where? what is always the same? what is different? what cant animals make some of? what are these called? how must they be taken in? what do all fatty acids have at one end? where is this the same as? what does the rest of the molecule consist of? whats this? how short or long can this chain be? whats the most common amount? draw a fatty acid molecule?
when is the term unsaturate or polyunsaturated often used? what is a lot of seen a poor diet? what do these terms refer too? what does it mean if all the possible bonds are made with hydrogen? what bonds bonds do unsaturated fatty acid have? so whats fewer? what does a sing C=C bong give? what does two or more C=C bonds give? what does introducing C=C also do? what does this shape change cause? making them more? what does this mean lipids containing many unsaturated fatty acids are often? but those with mainly saturated are? what do many animal lipids contain a lot of? what are they at room temp? what do many plant lipids contain? what are they at room temp? what are they caleD? the animal lipid lard is solid or liuid? what about plant lipid olive oil?
5%, fat, oil, can be respired to release energy to generate ATP, a source of energy, enegry storage, in adipose cells, cells that store lipid, lipids, lipid that reduces heat loss, insulation, provides electrical insulation around nerve cells, layer of lipid on the surface, protected against drying out, protection, lipids, steroid hormones, caron hydrogen oxygen, low, carbohydrates insoluable, are a diverse group of chemiclas that dissolve in organic solvent such as alcohol but not in watter thhhey incude fatty acids triglycerides and cholesterol
energy storage and supply, membranes, gycerol molecule, faty acid molecules, of the fatty acids they need from raw materials, esssential fatty acids, taken in complete as part of the diet, acid group, amino acids, hydrocarbon, a chain containing only carbon and hydrogen, from 2 to 20, 18,
when promoting the healthuer aspects of food, high in saturated fat, to the hydrocarbon chain and wether it is saturated with with hydrogen or not, the fatty acid is saturated, C=C, fewer hydrogen atoms can be bonded to the molecule, mono-unsaturated fatty acid, polyunsaturated fatty acid, the shape of the hydrocarbon chain, makes the molecules in a lipid push apart so makes them more fluid, oils, fats, saturated fatty acids, solid, fats, unsaturated fatty acids, liquid, oils, solid, liquid
Lipids are not polymers
What does a triglyceride consist of? are all fatty acids joined to glycerol molecules the same way? what reaction happens? where? what bond is formed? what is produced? whats the new bond formed called? whats the new molecule produced called? how is a triglyceride molecule formed? are they insoluable or soluable in water? what are they described a then? why? what does this mean? Draw the hydrolysis and condensation reaction for both moniglycerides and triglycerides?
One glycerol molecule bounded to three fatty acid molecules, joined the same way, condensation reactions happens, between the acid group of a fatty acid molecue and one of the OH (hydroxyl) groups of the glycerol molecule, covalent bond, water molecule, ester bond, monoglyceride, condensation reactions between acid groups of two or more fatty acid molecules with the two remaining OH groups on teh glycerol form a triglyceride molecule, insoluable, hydrophobic, charges on teh molecule are distriibuted evenly around the molecule, hydrogen bonds cannot form with water so the two dont mix easily
essentially what is a phospholipid identicle to? why? in phospholipids what isnt added where? what is bonded to what? what type of bond? how does the bonding occur? what is released? what is the phosphate head? what is the hydrocarbon chain fatty acid tails? are phosphilpis insoluable or soluable? what does the water-soluabilty of the head group give? are the fatty acids that make up a phospholipid saturated or unsaturated? what can organisms control then? give example? what does this ensure?
What does the respiration of lippids first require? between what? of what bond? what this the reverse of? what can both the glycerol and fatty acids be broken down completly to? what does this release? to generate what? does the respiration of one gram of lipid give more than one gram of carbohydrate? whats the significance of lipids being insoluable? what do these features make triglyceride an excellent? what does the respiration of lipids also give out a lot more than carbohydrates? what is this metabolic water vital to?
what is cholestoral a class of? what is not formed from? is it small or large? whats it made from? where is it found? what allow it to sit between the phosphloipid hydrocarbon tails? what does it also allow? name two steroids and one vitamin made from cholestorl? what does the lipid nature of the steroid hormones allow? where is this usually? so they can pas through what? where is cholestor especially made? what may be a problem? what can happen in bile? what can happen in the blood? causing what? which can result in? what does FHC stand for? what is it? why does this happen? what do they lack? what can people die fom? at what age?
i almost identical to a triglyceride molecule, a glyverol molecye with fatty acid molecules bonded by condensation reaction to produce ester bonds, the fatty acid to the gycerol molecke, phosphate group is covanet y vonded to the third OH group on the glycerol, codnensation reaction, water, hydrophilic, hydrophobic, insoluable, their charactertisics, saturated or unsaturated, the fludiity of the membrane, organisms living in coder cliamtes have an increased number of unsaturated fatty acids in the phosphipid membrane, reamin fuid despite the low temp
hydrolysi of the ester bonds holding the fatty acids and gycerol together, codnensatio reaction, carbon dixoide and waterm energy, ATP molecues, twice as much as carbohydrates, they can be stored in a compact way and they dont affect water poential of the cells contents, energy storage molecule, more water, some organisms
lipid, fatty acids and glycerol, small, four carbon based rings, in all biological membranes, its small and narrow strcute, to regulate the fluidty and strnegth of the membrane, testerone oestrogen vitamin d, pass directly through the phospohlipid bilayer to reach the target recptor, inside the nuceus so they can pass directy through the ipid bilayer of the nuclear envelope, liver, excess cholestorl, can stick togetger to form lumps called gallstones, be deposited in the inner lining of blood vessels cuasing atherosclerosis which can result in a number of circulatory problems, famiil hypercholestooralemi, genetic dirorder, cells manufatcure and secrete choesorl even though there is sufficent amount in the bood, cells dont obey signas to stop choelsorl reporuction as they lack a particular cel surface receptor, heart attacka and strokes, age of 2
Water a vital biological molecule
size of water molecules? what does it consist of? what bond? are the electrons shared evenly? what is the oxygen atom capable of? what does this mean water becomes? so what is water described as? define: hydrogen bonding? draw water molecule?
what do the hydrogen bonds do in pure liquid water? what do they form? what does it allow? doing what continually? what is made difficult? what does this exaplain then? how does this compare to similiar size molecules such as hydrogen sulfide (H2s)? what happens as temperature is reduced? more of what formed? do they break easier? what happens to the hydrogen bonds as water becomes solid? how did this form differ to liquid water? so what forms?
What do the hydrogen bonds in water restrict? so what is needed to increase temp? what does this mean for large bodies of water? what does the evaporation of water use? what does this mean water evaporating froma surface does? so what is used in evaporation?
why is water unusual? what happens as water cools? what happens at 4 degrees? what does this mean ice does in liquid water? what does it do to the water below? what does this allow organisms to do?
what does water on a waxys surafce almost look like? what doesnt it do? why is this? whats this property called? what happens? what does cohesion result in? seen where?
small, two hydrogen atoms and one oxygen atom, covalently bonded, are not shared evenly, puling the shared electrons towards it and so away from the hydrogen atoms in the molecule, slightly negatively charged at the oxygen end and slightly positivecharged at the hydrogen ends, polar molecule, a weak interaction that can occur wherever molecules contain a slightly nagativly charged atom bonded to a slightly positivly charged hydrogen, water molecules hydrogen-bond with each other extensivly,
form hydrogen bonds with each other, a network that allows the molecules to move around, making and breaking hydrogen bods as they do so, for water molecules to escpe the liquid to become a gas, exaplisn why water must be heated to 100 degrees before it boils, are gas at normal enviromental temp, water molecules move less becuase they have reduced kinetic energy, hydrogen bonds, break so easily, hydrogen bonds formed hold the structure in a semi-crystaine form, less dense,ice
the movement of the water molecules, reativly large amount of energy, this keeps the temp stable even when the temp changes dramatically, up a relativly large amount of energy, removes hat from the surface, heat energy
because its sold form-ice- is less dense than its liquid form, it density increases, then its density begins to dcrease again, ice floats on liquid water, insulates, to survive in winter and ive under ice
spherical, it hardly wets the leaf, the hydrogen bonding pull water molecules in at the surface, cohesion, water molecules sticking to each other, surface tension seen at the surface of a body
Water- a vital biological molecule
what does the soluabilty of substance in water depend on? what molecules will dissolve in water? whats the substance to be dissolved called? what charge does it have? what do they interact with? what do the water molecules do? what does this keep? what can happen one in soution? what is this the basis of? where does this take place? are ions charged? do they dissolve easily? why?
what does water remain over a large temp? what can it act as for many? what does this make it ideal for in living organisms?
State the 6 properties of water its importance and an example?
wether water molecules can ineract with it, polar molecues, solute, positive nd negative, ineract with water molecules, cluster around the slightly charged parts of the solute molecule, solute molecules apart so they are dissolved, molecules can move around and react with other molecules, metabolic reactions, in solution in the ctyoplasm, yes, easily, water molecules can cluster around them and seperate them
liquid, solvent, medium,
solvent- metabolic processess in all organisms relu on chemicals being able to react together, 70-95% of cytoplasm is waterdissolved chemcicals take part part in processess such as respiration and photosynthesis in living orgnaisms, Liquid-the movement of materials around organisms both in cells and on a arge scale in multicelluar organisms required a liquid transport medium- blood in animals and the vascular tissues in plants use water as a liquid transport medium, Cohesion- water molecules stick to each other creating surface tension at the water surface cohesion also makes long thin water columns very strong and difficult to break-trasnport of water in the xlyem relies on water molecues to stick to each other as they are pulled up the xylem in the transpirtation stream and some organisms use it to walk on water, Freezing- water freezes forming ice on the surface water beneath the surface becomes insulated and less likely to freeze-polar bears live in an enviroment of floating ice packs and lakes tend not to freeze so awautic organsism are not killed, Thermal stability- large bodies of water have stbale temp and evaportation of water can col surfaces by removing heat- oceans provide a relativly stable enviroment in terms of temp and many land based organisms use evaportion as a cooling mechanism e.g. panting or sweating, Metabolic- water takes part as a reactnt in some chemcial process- water molecules are used in hhydrolysis reactions and photosynthesis
Practical Biochemistry -1
What can confrim the presence of various biological molecules within a samplle? what do these test really indicate? what dont they indicate? what type of test is it known as then? what are these tests referred to as? why? what does the test rely on? what may be necassary for the test to work?
How can you show the prescene of starch? what happens if starch is present? what sort of sugar are monosaccharides and disacccharides known as? what does this mean? whats this known as? what is benedicts solution? ha happens when a reducing sugar is heated with benedicts oslution? what is the orange-red described a? why? what is this test called? do all sugars react with benedicts solution? what would happen? name a non-reducing sugar? how is it formed? out of fructose gucose and sucrose which ones are monosachharides and which are disaccharides? what is the difference between sucrose and maltose? why? what does this differnece prevent? what do you do if a substance doesnt react with beneicts solution? what do you do first? how? what does this do? what do you do next? by adding what? o? what are both of these? what do you carry out then? what does it mean if the test is positive? why?whats the heat temp for benedicts test?
what can you add to a sample to test for proteins? what test is this caled? wat coour is biuret reagent? what does it contain? what do these chemicals react with? found where? whats the result? does the test require heating?
What can you use to test for the prescene of lipids? what do you do first? whats ethanol what does this do? what are lipids in alchol? what do you do with this liquid? what happens if lipid is present? whats happened? define food tests?
a number of simpe chemcial tests, only the prescene of the the type of molecule not how much is present, quaitative, food tests, they can be sed to detect the prescen of the vaious biolgical moleculesin food sampes, grind or break up the sample,
add a solution of iodine in potassium iodie to the sample, iodine solution changes colour from yellow-brown to blue-black, reducing sugars, that a molecue can react with other moelces by giving electrons to them, reuction, alkaline copper sulfate, changes coour from bue to orange-red, orange-red precipitate, the orange-red substance comes out of the solution and forms solid particles dispered in the solution, benedicits test, some dont, negative test would show no colour change, sucrose, a condensation reaction forming a gycosidic bond between gucoes and fructose, fructose and glucose monosachahrides and sucrose is a disaccharide, the formation of the glycosidic bonds, the sucrose from reacting with the benedicts soution, you have to use a different test, make sure there is no reducing sugar in the sampe by boiling the sample with hydrochloric acid which hydrolyses any sucrose present by splitting sucrose molecues to give fructose and glucose mono then coo the solution and neutralise it by adding sodium hydrogencarbonate soution or sodium carbonate solution both are akais, carry out the reducing sugar test, the test wil now give a positive result because gucose and fructose are present 80 degrees,
biuret reagent to the sampe, biuret testm pale blue colour, sodium hyroxide and copper sulfate, peptide bonds found in proteins, iliac, no heating
ethanol emulsion test, mix the sample with ethanol, acloho, dossoves ant lipid present, lipids are souable in alchol, pour the liquid(alchol dissolved in fat) into water contained in another clean tube, a cloud white emulsion will form near the top of the water, lipid comes out of the solution and becomes dispersed as tiny droplets in the water
Practical Biochemistry- 2
what do the food test test for? what dont they test for? what sort of test do you need? define quantitative?
what does benedicts test reveal? whats the result? whats the resul like if theres more reducing sugar? what will be used more? how can the reamining solution be measured? what will this tell you? what can you estimate?
what is a colorimeter? what picks up the light? what will it give? where is the solution placed? between what? whats the container called? what does it mean if more cooper sulfate is used up in the benedicts test? what does the reading give then? how do you reset a colorimeter? what could increase accuracy?
what doesnt usuing a colirometer tell you about the differnet samples? what does it tell us? how do we quanitfy the amounnt? what must be taken first? whats plotted against what? what is finding thhe concentration of a substance in a sample and comaoring it with known standards known as? define assay?
prescene of various molecules, how much is present, quantitative test, test that gives measurment of a substance in units not simply an indication,
if reducing sugars are present, orange-red precipitate, the more precipitate will be formed, copper sulfate, the more beneficts solution will be used up, the precipitate must be filtered out, how much benedicts solution has been used, the concentration of reducing sugar in the original sample,
a device that shines a beam of light through a sample, a photoelectric cell, a reading shwoing how much light has passed through the sample, a sample chamber, the light and the photoelecric cell, clear plastic container, cuvette, the less light will be blocked out and the more light transmitted, gives a measure of the benedicts reaction, blank sample with 100% transmision like water, colour filters
does not tell us how much reducing sugar is present, which sample contains more, a calibration curve must be drawn, take a range of known concentrations of reducing sugars, transmission against reducing sugar concentration, assay, techniuqes are often used to compare measurements with known samples so that quantitative measurements can be made
Nucleotides - coding molecules
what two forms do nucleic acids come in? what do they stand for? what do these molecules hold? where is almost all DNA found in a eukaryotic cell? what does the nucleus act as? how many forms is RNA found in? what are these forms needed for? to produce what? what are they required for?
What is the monomer of all nucleic acids? what is each nuceltotide made up of? what reaction joins these three? where joins to what? what bonds are formed? define: nuceltoide? draw a nucleotide?
How many differnet nucleotides? what do they code again? what is always the same in the nucleotide? what is carbon is the sugar? is it deoxyribose or ribose? what varys? what can they be?
what reaction joins nucleotides? between what and what? how is a long chain made? what does the backbone of this chain consist of? what projects from the backkbone? what codes the information then?
what are chains of nuclotides bonded together called? what will only bind with what in the long chain polymer? whats the result?
what can the five organic basis be grouped into? whats smaller? which bases go into which group?
what is produced when excess pruines are broken down? where are they broken down? how is it excreted? what do some people have? whats wrong with it? at what temp? whats formed? deposited where? like? what does the toe become? whats this condition called?
DNA and RNA, deoxyribonucleic acid and ribonucleic acid, the coded inform to build that organism, found in the nucleus, information store, three, read and translate the information, produce various proteins required to make the living functioning organism,
nucleotide, three joined subunits- one phosphate gorup one sugar molecule and one organic nitrogenous base, condensation reaction, phosphate to deoxyribose to base, covaent bonds, are the monomers of all nucleic acids each nucleotide is formed by bonding together a phosphate gorup a sugar molecule and anitrogenous base,
4, the instructions to make proteins in all living things, phosphate group, 5-carbon sygar, deoxyribose in DNA or ribose in RNA, the nitorgenous base, adenine thymine guanine cytosine uracil,
condensation, phosphate group of one nucleotide and the sugar of another nuelotide, by reapting this bonding, repeating sugar to phosphate chain, nitrogenous base, it is this sequence of various bases,
nucleic acids, only nucltotides carrying the same sugar, this means there is either ribonucleic acids (RNA) where the sugar is ribose or deoxyribonucleic acid (DNA) where the sugar us deoxyribose
into two groups, pyrimidines and purines, pyrimidines, Purines- adenine and guanine, Pyrimidines-thymine cytosine and uracil
DNA- Information storage
What is DNA made up of? what is the polymer chain called? when is a DNA molecule formed? what does the sugar phosphate backbones form? what do the bases do? to form what? what bond forms between the bases? what does this do for DNA molecule? why is this vital? what if it were unstable?
Why do the strands run parrallel? why is the term antiparrallel used? how are the sugars pointing? are the chains always the same disatnce apart? why? what appears on the oppisite side of a pyrimidine? what appears opposite adenine? what appears opposite to guanine? what forms between the bases? how many between A and T? how many between C and G? what does the different struture of the bases mean? what is the base pairing described as? so whats complementary to what? in a complete DNA molecule what do the antiparrallel strands do? whats formed?
during cell division what must each new cell recieve? what must each cell have? what does this mean the cells need? when does this DNA replication happen? what happens first to make anew copy of a DNA moecule? what is broken? what does this do? whats exposed? whats is bonded onto the exposed bases? still following what rule? where are covalent bonds formed? what is sealed? how long does this continue for? what is each? why? whats this repkication process called? why? what is semi-conservative DNA also responsible for? define: DNA?
What is the sequence of bases an example of? where is the information? whats the significance that the molecules are long? what does the base-pairing rule allow? what does the double helix structure give? what do the hydrogen bonds allow?
a long chain of nucleotide monomers, polynucleotide, when two polynucleotide strands come together, the uprights, project towards each other, rungs, hydrogen bonds, strengths the rungs and makes DNA a very stable structure, the insturctions could go wrong easily
because the sace between them is aken up by the nitrogenous bases projecting inwards, because the strands run in opposite directions to each other, in oppisite diretions, always the same distance, because the bases pair in a specific way, purine, thymine, cytosine, hydrogen bonds, 2, 3, the base-pairing rules always apply, complementary, A to T and G to C, twist around each other to form the final structure of a double heix
must recieve a full set of instructions, a full copy of all the DNA for that organism, a way of copying DNA strands precisly, in interpahse in the cell cycle, the double helix is untwisted, hydrogen bonds to unzip the DNA, the nitogenous bases, free DNA nucleotides are hydrogen bonded, base pairing rule, between the phosphate of one nucleotide and the sugar of the next to seal the backbone, all the way aong the molecule untill two new DNA molecules are formed, an exact replica of the orignal DNA molecule because of the base-pairing rule, semi-conservative repication, one conserved strand pluse one newly built strand, for the production of new DNA molecules, DNA is a stable polynucletide molecule it acts as an information store because the bases projecting from the backbone act as a coded sequence organisms differ in their DNA inly because they contain differnet sequences of bases in the DNA
information storage, is in the form of codes to build proteins, lagre amounts of information can be stored, complementary strands of information can be replicated, the molecule stability, allow easy unzipping and copying and reading information
Reading the Instructions
whats the differnece in the sugar molecule in RNA to DNA? whats the differenc ein bases? whats the differnece in the polynucletoide? whats another difference?
What do RNA molecules never contain? what bases make RNA then? what do hydrogen bonds form in RNA? so what still takes place? what does the base pairing also make complementary to each other? why is this? what can the sugar-phosphate do? what is this the basis of?
What are the three forms of RNA? what is mRNA complementary to? what strand? what is it therefore? whats this strand? where rRNA found? what does tRNA carry? to where? to do what? what is the chain of tRNA stablised by and where?
what do the sequences of bases on DNA make? what do they code? what is a gene? how can the sequence coding for a gene be exposed? what is formed on the exposed gene? what do they become? what is the mRNA now? what does the mRNA do then? what does it attach to? what does tRNA bring? accoridng to what? what are the amino acids joined by? to give what? what will it have? what does this rise to?
the sugar molecules that makes up the nucleotide is ribose not deoxyribose, the nitrogenous base uracil is found instead thymine, the chain is single stranded, three forms exist,
the nitrogenous base thymine, adenine uracil cytosine and guanine, hydroge bonds forms between c-t and then a-u, base pairing, RNA can be complementary to molecules of DNA, because exposed DNA nucltotides can have free RNA nucleotides hydrogen bonded to them, then then sugar-phosphatte backbone is sealed, of copying gentic code of the DNA base sequence, transcription
three forms, one strand of DNA molecule, template strand, a copy of the other DNA strand, the coding strand of the doublie helix, ribosomes, amino acids to the ribosomes, where they are bonded together to form polypeptides, the chain folds and is stabalised by hydrogen bonds as complementary bases come near each other
codes for a particular protein molecule, the sequence of amino acids in the protein, a gene is a length of DNA that codes for one or more polypeptide each gene iccupies a specific locus on a chromosome different versions of the same gene are called alleles, by splitting the hydrogen bonds that hold the double helix together in that region, RNA nucleotides, mRNA, is a copy of the gene, peels away from the DNA and leaves the nucleus througha nuclear pore, attacthes to rRNa in the ribosomes, bring amino acids to the ribosome in the correct order, to the base sequence on mRNA, peptide bonds, a protein, primary structure, secondary and tertiary
Enzymes are Globular Proteins
what do all globular proteins have? where does the shape come from? which is? and also its? in globular proteins whats at the centre? where are the hydrophilic amino acid R-groups? what does the amino acid chain do to form the overa structure? whats similir about enzymes? what are they in water then? what do they act as? meaning? how are they specific? what does the globular structure contain? called? what is their activity affected by?
describe the size of enzymes? how many amino acids do they consist of? what are the majoirty of them invovled in maintaing? what is the enzyme function related to? like all of what? for an enzyme to work what needs to be maintained? esssentialy what is the whole primary secondary and tertiatry structure of enzymes invovled in? for what? what is the active site? what does each enzyme have? mainited by what? out of the hundrds of amino acids how many form the actual active site? as the active site is specific what doe this mean the reaction an enzyme can catalyse is?
what are enzymes sometimes refreed to as? what do they do? what do industrial and commercia catalysts include? how do they compare to enzymes? what investigation has this lead to? whats the added advnatge of enzymes?
where are chemica reactions that are catalysed by enzymes? what can be described as enzyme driven?in looking at biological molecules what bonds have been explored? what does each of these require? what does the enzyme do? name other bodily process that require enzymes? what does each enzyme catalyse? whats the estimation for the amount of enzymes in each cell?
specific tertiary structure, the specific sequence of amino acids that form the primary structure, secondary structure, hydrophobic amino acid R-groups, around the outside of the ball, spirals pleats and turns, they are globular, soluable in water, catalysts, speeding up chemical ractions but not being used up as part of the reaction, catalysing a reation involing only one type of substrate, cleft area called an active site, temperature and PH,
quite large, hundreds, the tertiary structure of the enzyme, related to shape, all protiens, teriatry structure must be maintained in a very specific way, invovled in achieving a very specific shape for the active site, the area of the enyme where the catalytic activity of the enzyme occurs, a very specific individual shape, specific overall tertiary structure, fewer than 10, the reaction an enzyme can catalyse is also very specific and indivual
biolgoical catalysts, speed up chemical reactions without being used up themselves, metals and other chemcials, they are rather slower, to use enzymes in industrail process to repalce such inorganic catalysts, they are specific to one reaction and dont producea range of unwanted by-products
withing and sometimes outside of cells,metabolism, glycosidic ester and peptide bonds, require at least one specific enzyme, in order to catalyse the reaction, protein synthesis digestion respiration and photosynthesis, a specific reaction in the sequence of events that make up the process, 1000
Enzymes are Globular Proteins
in a chemcial reaction that is cataysed by an enzyme what is turned into what? name an enzyme? what conversion does it catalyse? what is the substarte? what is the product? draw the equation? how are enzymes given their name?
what does the enzyme lactase catlayse? into what? what are they? what dont lactose intolerent people produce? what happens? what does catalase catalyse? to what? why do almost all organisms produce catalase? what do plants need carbon dioxide fo? what does the enzyme rubisco do? what does ATP-ase catayse? to what? what does this reaction release? that is used for what? what does glycogen synthetase catalyse? how? what is glycogen?
substrate is turned into product, malase, catalyse the conversion of maltose to glucose, substrate is maltose, product is glucose, maltose --->(maltase) glucose +glucose, dereived from the substrate that is catalysed with "-ase" on the end,
the breakdown of milk and sugar (lactose) into glucose and galactose molecules =, dont produce lactase and suffer stomach cramps bloatin etc if they take in milk products, the break down of hydrogen peroxide to water and oxygen gas, because hydrogen peroxide is a toxic by prodyct of some metabolic reactions, for photosynthesis, the binding of carbon dixiode to a molecule called ribulose bisphosphate, the breakdown of ATP to produce ADP and a phosphate group, a small amount of energy that is used to drive energy requireing process like active transport, the building of glycogen, by catalysing the joining of glucose molecules, the storage carbohydrate of animals
Inside and out - where enzymes work best
what do all organisms on Earth use enzymes for? what are all enzymes? what is their weakness then? what are organisms able to live in? why?
whats an endothermic animal? what are they able to do? give examples? what allowed them to do? what does regulating body heat mean for enzymes? whats the problem though? what do birds and mamals require that reptiles dont? whats the advanatge of having enyme activity at continous and optimum level?
what are hetertrophs? what do these organisms need to do extract the nutrient molecules they need? what do they need them for? what does digestion involve? what needs to be broken? name three? whats is this catalysed by? what do some organisms secrete? onto what? what does the enzyme do?what can the organism then do? where are other organism digestive sytsems? what happens to their food as it pass through the digestive system? what are enzymes in digestive systms also? how? where are other enzymes found? what are these described as? why?
why are enzymes that catalyse reactions to break down molecules useful tools? what do they uses enzymes as? what do white blood cells take in? what type of white blood cell? whats in the endocysted vesicle? what does it fuse with? what digest the bacterium?
to catalyse metabolic reactions, protein molecules, for an enzyme to work its shape must remain intact, able to live in a wide variety of enviroments, only because they are adapted to dea with differnt enviroments because their enzymes continue to function
an animal that produces heat from its cells when it respires to maintain a constant body temp, maintain their internal body temp indepoendalty of the enviroemnt, birds mamalls, to live in most of the differnt enviroments in the world, enzymes can function at near optimum temperature inside the organism, high energy cost, they require a much greater food supply then similiary sied reptiles, have allowed endothermic animals to survive very well both land and water
organisms that obtain their nutrients by consuming other organisms, need to break down the body of the irganism they are consuming in order to extract the nutrient mlecules thy need for growth and energry requirements, breaking down larger molecules into their subunits, breaking of bonds, glycosidic peptide ester, catalsyed by differnt types of enzymes, enzymes outisde the body, onto the food source, digest the molecule into their monomers, which the organism can then take in and use, internal digestive system, various enyzymes are mixed with it in order to digest the nutrients it contains, extracellular, releaed from a cell that make them, onto food withing the digestive system spaces, cytoplsm of cells or attached to cell membranes, intracelluar, their actions take place inside cells
protecting organisms, defence mechanism,invading microbes like bacteria, phagocytic, bacterium, fused with one of the many lysosomes, lysomal enzymes
Do covalent bonds just assemble and break easily? why? Maltose example- what is maltose made up of? joined by what? what reaction spits maltose? what needs to be broken? at the same time what else must be split? where must the split parts of water go? to reform what? how can this reaction in a test tube? what does this provide the right conditions for? what is the extra energy required to enable the reaction called? define: activation energy?
what are biologicla molecules to stable for? what does boiling in acid give? what is destablised? what happens when it collides? whatts wrong with cells boiling water and acid? what does it need then? to drive what? without catalysts what would never happen?
what do enzymes reduce?what do this mean can proceed? how can they do this?
what does an enzyme have? what is the active site complementary to? what does this mean for the substrate? what term is given to this fit? what do we now think hod? what do we also believe about the charges of amino acids?what is this called? can the same enzyme catalyse the reverse of the break?
what happens as the substarte collides with the active site? what does this make? as the substrate fits what holds it? whats this called? what can this change in shape cause? what does this do to the substrate? what does this mean for the reaction? whats produced? what is it now referred to as? how are the products differnet? do the products still fit? what do they do? what is the enzyme ableto do now?
no, they are far to stable, two glucose molecules, glycosidic bond, hydrolysis reaction, the glycosidic bonds, a water molecule, must bond back onto the split parts of the maltose molecue to reform glucose molecules, can be boiled with acid, for maltose to collide with water molecules energtically enough to achieve hydrolysis, activation energy, is the amount of energy that must be applied for a reaction to prroveed different reactions rquire differnt levels of activation energy enzymes reduce the amount of activation energy needed to allow a reaction to proceed,
to break up or self assemble uner conditiosn found in the cell, gives molecules a great deal of extra energy, to destablise the structure of the molecyle, the reaction proceeds, the cell will not survivie, catalysts (enzymes) to drive its metabolic reactions, metabolic reactions could not occur
reducing the amount of activiation energy required, this means that reactions quickly at temperatures much lower than boiling point, because of the way the active site is shaped to fit the substarte molecule or molecules
specifically shaped active site, compementary to the shape of the substrate molecule inolved in the reaction, substarte molecule is smaller so it can fit, lock and key, changes in the shape of the enzyme occur as the substrate binds to the active site, that the charges on the amino acid in the active site also contribute to holding the substrate so that the reaction can occur, induce-fit hypothesis
the enzyme molecule changes shape slightly, the active site fit more closely around the substrate,because oppositly charged groups on the substrate and the active site are found near each other, enzyme-substarte complex, place strain on the substrate molecule, occurs more easily, a product, enzyme-product complex, theyre a different shape, no longer fit, move away, now able to catalyse the same reaction with another substratte molecule
Enzymes and Temperature
what do the molecules in gases and liquids do continually? what do they have? what do these movements mean? what happens if a gas or liquid is heated? what do they do? what happens more often? and what does it mean when they do collid? why?
when can enzymes only catalyse a reaction? so what is formed? what is it important to remeber? what if the kinetic energy of both enzyme and substrate are increased? whats is increased? what is more of formed?
other than make them move faster what does heating also do to molecules? what do these vibrations cause? in large molecules like enzymes what can be broken? what sort of bonds? how do these weaker bonds occur? what structure are they responsible for holding together? in particular which part of an enzyme? as heat is incresed what is also? what does the teriatry structure become less and less? what will happen to the rate of reaction? what will happen if enough of these bonds are broken? like all proteins what if the tertiary structure is significantly? is this reversible? why? whats this called? define: denaturation?
what does increasing the temperature do for the reaction speed of an enzyme cotrolled reactin? what happens as the temp increases further? why? what does optimum temp mean? whats it a balane between? what does measuring the effects of temp? using what? what can be measureD?
What do most enzyme have an optimum temp of? what would these enzymes be for some organisms? what must these enzymes have to live in the temps they do? what are heat resistant enzymes used for? whats the process known as? whats it similiar to?
move around continually and randomlly, natural kinetic energy, continualy collide with each other, kinetic energy is increased and they move around more quickly, colission between the molecules more often, they collide with greater force as they are moving faster
if a substrate molecule(s) collide with the active site of the enzyme, enzyme-sibstrate complex, that the random movements of enzyme and substrate lead to these colissions, there will be an increased number of collissions between enzymes and substrates, more collisions between enzyme, rate of reaction, more products are formed
it makes the molecules vibrate, strain on the bonds that hold the molecules together, break the weaker bonds, hydrogen and ionic, they occur in larger number, for holding the tertiary structure in place, maintain the active sites shape, more and more bonds are broken, in the shape needed to keep the active site in its working form, decrease, the whole tertiarty structure is changed significantly, cant function, even if temp is lowered the tertiary structure is to to damaged to rebuild, denaturation, changes the teritary stricture of an enzymes such that it cannot function and it cant be restored it doesnt change the primary structure of an enzyme or any protein
the rate of reaction at first, the rate of reaction decreases, the enzymes stop working, enzymes optimum temperature, between kinetic energy (which increases the number of collisions) and increasing the vibration of the enzyme molecule (which breaks the bonds that hold the tertiary structure in place) carrying out enzyme-controlled reactions at differnt temps, water bath controled by using a therostat, the production of product or disappearance of substarte
between 40 and 50, for some organisms they would be useless, heat-resistant enzymes, used to catalyse ractions invoved in maakingcopies of DNA, polymerase chain reaaction, DNA replication
Enzymes at work- ph effects
what is ph a measure of? what do ph values range from? what is neutral? what is below and above? what does it mean the higher concentratpm pf H+? what does this mean acids contain? in chemical terms what is an aacid defined as? why?
What does a hydrogen ion carry? what will it attract? what will they repel? what holds the teriary structure of enzymes and proteins in place? where in the structure? what does this in turn assure? what are these bonds due to? what can interfer with the hydrogen bond and ionic bonds? how? what can this result in? what can increasing or decreasing the concentration of hydrogen ions around an enyme alter? what can changes in PH cause? and change the rate of what?
what does the induced-fit hypothesis state? what will increasing the concentration of hydrogen ions do? why? what does this interfer with?
what do all enzymes have of their own? what is this? what is the most common? what does the optimum ph give the tertiarty structure? what does it do for the active site? what is the shape? describe the range of ph that enzymes work best at? what is chaning the ph really? what can even slight changes result in? why? what does mesauring ph involve? what can be measured?
why do differnet enzymes have different optimum ph levels? where is pepsin found? whats its ph? why is this ideal? whats a protein digesting enzyme called? wheres it found? whats its optimum ph? why is this ideal?
the hydrgen ion (H+) concentration, 1 to 14, 7, below is acid and above is alkaline, lower the ph, s high concentration of H+, proton door, because the hydrogen ions are known as protons,
positive charge, , negativly charged ions molecules or parts of molecules, positvly charged ions molecules or parts of molecules, large number of hydrgoen and ionic bonds, the active site is held in the right shape, attraction between the oppistely charged groups on the amino acid that make up the enzyme (protein), hydrogen ions, because of their charge, the tertiary structure of the enzyme molecule, changs to the shape of the active site and so the rate of enzyme-controlled reaction
states that an important part of catlysis in the active site relies on the charged R-group of the amino acids that make up the active site, the charges around the active site, H+ are attracted to the nagtivly charged group and so cluster around it, with binding of the suvstrate to the active site,
optimum ph, the ph at which the rate of reaction is highest, neutraul 7, the concnetration of hydrogen ions gives the tertiary structure of the enzyme the best overall shape, holds the active site in the best shape that fits the substrate, complementary, narrow range,altering the cocnentration of hydrogen ions, result in a fall in the reaction rate because th shape of the enzyme molecule is disruoteed and so te shape of the active site changes, enzyme controled reactions at differnt ph vaues using buffer soutions, production of prodct disappearance of a substrate
because thw wide range enzyme sappear have a range of PH levels, stomach, protein digesting enzyme, 2, stomach contains hydrochroic acid, trypsin, small intestine, 7, ideal for the samll intestine enviroment
Enzymes at work- Concentration effects
in experiemnt situatioons what can the concentrations of a substarte be? for what? what if theirs no substarte? why? whta happens s the concentratopm pf substarte incresaes? what is more formed of? so what is more formed? what happens to the reaction rate? what happens if the substarte concentration increases furhteR? whats happening at this point? iin effect what are all the active sites? what effect will increasin the substrate concentration then?
what can the concentration of an enzyme be in experimental situations? for what? what increases if the enzyme concentration does? what are more formed? what is more produced? what does the reaction rate do? what happens if the enzyme concentration icreases furher? what is the reaction rate at? what does increasing it further do?
in an experimental situation when will the enzyme controlled reaction be at its highest point? what is is increased? what decreases as time passes? what frequeny goes down? what decreases? what is the highest reaction rate known as? what does it give?
what is the levelling of on a graph known as? why does it occur what are they doing? what are they described as? what happens if the concentration of the limiting factor is increased?
in cells what are the enzyme concentrations? why is this partly because? what is the control of metabolism based on? name one way of regukatibg enzyme activity?
can be varied for a fixed concentration of enzyme molecues, the reaction cannot proceed, becaus enzyme-substrate complexes cannot be formed, collisoon between enzyme and sibstare molecules occur more often, more enzyme-substarte molecules form, more product is formed, the rate of reatcion increases, a point will be reached where the reaction rate reaches maximum value, all the enzyme moleules present are forming enzyme-substrate complexes as fast as possible, all active sites are occupied, will have no effect on rate of reaction
is varied for a fixed concentration of substarte molecules, more active sites become avaiabe, more enzyme-subsrarte molecues are formed, so are more prodts, rate of reaction increases, a point will be reached where all substarte molecules are occuping enyme active sites, is the maximum possible for the fixed substaret concentration, wont effect reaction rate,
when enzyme and substrate are mixed, product mlecules are formed and inceased in nunber, substarte is used up and decreased, goes down and so does the rate of reaction, inital reaction rate, gives the maximum possible reaction rate for an enzyme under a particular experimental situation
plateu, becayse either enzyme cincnetration or substarte concentration prevents any furhter reaction rate, limiting the reaction, limiting factors, the reaction rate increases,
relativly low level, enzymes being catlysts work over and over again driving the same reaction, is based on the control of enzyme activity, is by adjusting the concentrations of enzymes and or substartes
Enzymes at work - inhibitors of actions
what are inhibitors defined as? why? is their a range or are they the same? what do some just effect? what do others effect? is it directly? how? how many enzymes can some inhibots affect?
what do competitive inhibitor molecues have? what does this mean they can do? forming what? what do these complexes lead to? why? what doesnt happen to the reaction? why does enzyme inhibiton occur? so what is reduced? what is therefore reduceD? whatt does the level of inhibiton depend on? what if substare concentration increases? why?
what do non compeitive inhibots not do? what do they do instead? what is distorted in this attacthment? what does this therefore distort? what no longer fits? what cant be formed? what happens to the rate of reaction? what does the leevel of inhibiton depend on? what if there are enough inhibots to bind to all the enzyme molecules? what will chanign the sibstaret conenctration do?
do most compeitive inhibots bind permeantly? how long? what is their action described as? why? do non compeitive bind permeantly? what are enzymes effectlvy? why is inhibiton sometimes good?
subsatnces that reduce the reaction rate of an enyme-controlled reaction, they have some effect on the enzyme molecule, wide range of enzyme inhibots, some effect the active site of just one enzyme, others affect parts of the molecule, indirectly, cayusing a change in the shape of the active site, a number of different enzymes
to that of the sustrate molecules, they can occupy the active site, enzyme-inhibitor compelxes, dont lead to the formation of products, the inhibtor is not identica to the substrate, is not catalysed, whenever an inhibotr molcules is occupying an enzymes active site, a substaret cant enter, enzyme-substtrate complexes is reduced, reaction slows down, on the concentrations of inhibotr and substarte, level of inhiiton decreases, substarte molecules is more likely than an inhibtor molecule to collide with an active site,
dont compete with substrate molecules for a place in the enzymes active site, they attatch to a different region from the active site, distorts the tertaiary structure, change in the shape of active site, substrate, enzyme-substarte complexes cannot form, rate of reaction decreases, on the number of inhibitor molecules present, then the enzyme-controlled reaction will stop, no effect on this form of inhibiton
not permenntaly, short period of time and then leave, reversible, remova of the inhibitor from the enzyme has no lasting effects, many bind permeantly, if it stays not rversible, denatured, the reguation of a number of metabolic pathways invoes the inhibiton of enzymes to control the reaction rates
Enzymes at work- coenzymes and prosthetic groups
when can some enzymes only catalyse a reaction? what can ensure that enzyme-controlled reactions can take place at an appropriate rate? what are these substances knownas?
what are coenzymes? what do they do? for how long? when do they bind? what do coenzymes do in many reactions? what happens to them like substartes? how are they unlike substrates? what is the role of co-enzymes often? so they do what? what is vitamin B3? what important role does it play? what is this viitaimin used in the body to make? what is that required for? what does pyruvate dehydrogenase catayse? what cant happen without vitamin B3? what can it result in if you dont have it in your diet?
what is a coenzyme that is ppermanent part of an enzyme molecule calleD? where are these also found? what are they vital to? what do they contribute to? and to what of the molcule including what?what does the enzyme carbonic anhydrase contain? where in the body is this enzyme vital? what does it catalyse? to produce what? why is this reaction importna?
what can increase the rate of reaction in some enzyme-controlled reactions? what can ions combine with? whatd does the binding of the ion result in? why? what does the enzyme aylase catalyse? to make what/ when will thsi enzyme only function propery?
if another non-protein substance is present, a number of diifferent substances, cofactors,
smal organic nonprotein molecules, bind to the active site, short period, either before the reaction or during when the substarte binds, they take part in the reaction and are changed in some way, coenzymes are recyced back to take part in the reaction agai, to arry chemical groups between enymes so they link together enzyme-controlled reactions that need to take place in sequence, micotinamide, heping the body break down carbohydrates and fat to release energy, to make a xoenzyme that is required for the enzyme pyruvate dehydrogenase to function properly, catalyses one of the reactions in the sequence involved in respiration, normal growth and deveopment, pellagra
prosthetic group, in other protein molecules, to the function of the enzyme or protein, contribute to the final tertiary structure, the properties of the molecule, its charges, zinc based prosthetic group, red blood cells, the combiing of carbon dioxide and water tp produce carbonic acid, that enabes carbon dixoide to be transported in the blood,
certain ions increase the rate of reaction, the enzyme or substarte, the enzyme-substaret complex form easily, it affects the charge distrubition, the shape of the enzyme-substrate complex, the breakdown of starch to maltose molecues, chloride ions are present,
Interfering with enzymes- poisons and drugs
how do many poisonious substances have their effects? give exampe? what does itnhibt? why does it do this? for what? whats it called? found where? what does inhibiton of this enzyme cause? wat cant be made? how can organisms only respire? what does it lead to? how much cyanide can be absorbed before an adult loses conciousness? how fast can this hapen? what does the body do? in how long? what happens eventyally? how long? what is infection by viruses treated using? how do they help? what do the viruses need these for? what do the protesae inhibtoirs specifically inhibit? often as what inhibitor?
what is one of the symptoms of the genetic disase cystic fibrosis? what does this mean indivudas have probels with? what do doctors prescribe? what are the enzymes packaged with? so what doesnt happen?
where is ethylene glycol found? is it poisonous? what happens if its taken into th body though? by what enzyme? whats the breakdown product? is that poisonous? what can it lead to? if someone does intake what are they given? what does this lead to? whats the benefit? what does the ethanol act as? of what? what does this reduce? allowing what?
becuse they inhibit or even overactivate nezymes, potassium cyanide inhibits cell reespiration, non-compietive inhibitor for a vital respiratory enzyme called cytochrome xidase, mitochondria, decreases the use ofoxygen soo ATP cannot be made, repsire anareobically, build up of lactic acid in the blood, 200-200mg, 10 secs, coma in 45mins, death 2hours, chemcials that act as protease inhibitors,virusese from replicating by inhibitng the activity of protease which the viruses need in orde rto build new virus coats, inhibit the viral protease enzmes often as compeitiv inhibitors,
passage of digestive enzymes normaly secreated from the pancreas into the gut is blocked, digesting good, enzymes in table form, packaged in acid resistnt coats so that theya re not destroyed by the acid and protien digesting enzymes in the stomach
antifeeze used in car engines , its not posionous, if in the body it is brojen down by the liver y the enzyme alcho dehydrogenase, oxaic acid is extremly toxic, lead to death, be given massive dose of ethanl, achol, to sever achol intoxication, compeitive inhibitoe of alchol dehydrogenase, reduces the rate of production of oxalic acid, alowing the ehtylen glyco to be exctred harlessy
Investigating enzyme action - 1
What are enxyme inestigations usualy? what happens in an enzyme controlled reatcion? what can an in vestiation into enzyme activity follow the rate of? or the rate? give a measure of waht?
investigations into enzyme actiivty meaure how many variabes? give example? what is the vriabe that i set by the investigator? what is the variable measured by the investiator? why is vital that the independant vairable is set precisily? what should the inevstigation choose good raneg of? whats the min what is esential? why? what is seperating rhem and getting hem a the right mep called?
what varibees cahnge and waht stay the same? what ar ethe key vraibles in enzyme control? whats the method of finding temp? why not room temp? why a wate rbath? what wont the reuslts reflect? give one method of testing enxzyme contcentration? whats the reason here? what if its in a liiving tissue? what must be assumed in living tissue? what if your using the whole tissue? what will effect reaction rate what if the SA is different? method of substarte conenctration? resons?method if ph alue? reasoons?
what ar ethe two main wyas of measuring the reaction ate? what must be used? how quick are they? so its over a period oof ? wgie formua for reaciton rate?/ what may be necassary to incude? what would you usally use? what does the contro show?
pracical assessments, enzyme catayses a reaction where substarte is turned into prouct, rate at which substrate is used up or the rate at which product is form, rate of resaction,
one varuabe, rate at which product is formed, against variation in temp, independant variable, dependant variable, otherwise readings of the depeendant vrible are meaningess, good range for the independant vairae, 5, enzyme and substrate are the same temp, not give orecise in the reacting mixture, equilibiurm,
the vraibe being investiated changes everything else stays the same, temp enzyme constration substarte concentration ph, kept constant by carrying out enyme controlled reaction sin a bath with a theromstat if not possible use a polystyrine seeve as insulation, is to varubae, fluctuations in temp wil afecct the reaction so readings wont reflect that variable, use accuraty measured vilumes of enzyme soution, concnetration of enzyme molcules present accuracy gives a constant concnerrton of enyzme molecyes, accurate measuremnets of the mass you msut assume tht all oeces contain the same number of enzyme, surface area the same as well as mass, the number of enzyme molecules in contact with the substarte wil affect the reactionmm accuractly measre volume mass of susarte, depends on cencentration of substarte molecules, PH buffers solutions tha tmainta PH at a set level, depend on ph because of its effect on the shape of the active site
start the reaction then measure concentration of product after a fixed period or monitor the reaction by taking reading of the product formtion at a number of time intervals, suitable time scale, quickly, seconds, reaction rate= 1/time, cotrol, water, that it is the enzyme actionr ather than any other fcator tat affects the reaction
Investigating Enyme Action-2
hwhat is formed in enzyme controlled reactions? what will these product molecules colide with? what happens to the rate?hows it best to show the effect of any dependant varible on the action of the enzyme? how can you do this?
how many times should a investiation be repeated? what should this give? who could you cpmare with?
product moecules, also collide with enzye moecues, reaction rate slows, it is best to compare the intial reaction rrates at each vaure for the dependant variable seeral readings over the course of the rreaction potting a groph of poruitc formed or susbatrte used take a tangent of the steepest portionn for a measure of the inita reaction rate,
3, should give the most accuarte resut, cassmates, you may have been doing something wrong
Enzymes and Metabolism- an overview
what couldnt happen withou enzymes? what do enzyme increase? whats the limit to the reaction rate set by? what must the power of enzyme be though? why? what could uncornteolld enzyme actiivty be? give exmape?
what do metabolic processess involve like? whats the product? wat are these sequnces caled? what is vital doesnt happen? wahat can happen? whats this the same as? where does it bind? what cjabges? what reduces?
what are some enzymes vital for? like?
what are all enzymes? whats needed then? in what form? whats meant by faulty? what if its faulty? what may be caused? what are they caled? h
metabolic reactions could not conitnue at thea rate high enough enough to support living porcesses, reactin rates, how fast the subtarte collides with the active site, controled, specific amounts, dangrous, mulitple sclerosis,
series of enzyme controlled reactions, respiration photynthesis, the product of one enzyme controlld reactions is the substare for the next enzyme contrled reactionmetabolic pathways, product doesnt build up, attach to one enzyme earlyier in thes equence, reversible non compeitivie inhibiton, part of the enzyme away from the active site, changes the shape of tha ctive site, reduces the rate,
vital to life, atp,
protiens, must have instrctions to make the enzyme needs DNA, mutated, then the enzyme may not be made correctly, diseases, inobrn erros of metabolism