Biological molecules
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- Created by: sarah
- Created on: 24-05-14 14:12
Define Biochemistry
the chemical reactions involving biological molecules
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define metabolism
the sum of the total of all the chemical reactions that take place in an organism
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Define organic chemistry
the study of chemical reactions that involve carbon
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why are covalent bonds strong and stable?
share electrons filling outer energy leve, meaning it takes more energy to break them down
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define Monomer
single, small molecule, many of wich can join together to make a polymer
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define polymere
a larger molecule made up of many repeating smaller molecules (monomers) covalently bonded together
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what are carbohydrate monomers called?
monosaccharides
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what are carbohydrate polymers called?
polysaccharides
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what are protein monomers called?
amino acids
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what are protein polymers called?
polypeptides
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what are nucleic acid monomers called?
nucleotides
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what are nucleic acid polymers called?
DNA/RNA
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what do we use nucleic acid for?
information molecules
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what is water used for?
transport, support plants, reactions, solvent
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what are carbohydrates used for
energy store and suply (e.g starch), structure (e.g cellulose)
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what are proteins used for?
structure, transport, enzymes, antibodies, hormones, membrane cariers/channels
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what are lipids used for?
cell membranes, sources of energy, stores of energy (adipose tissue), some hormones (steroids), protection (leaves and organs), insulation (thermal and electrical)
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what substances make up 99% of organisms?
carbon, hydrogen, oxygen, nitrogen
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what is the term used to describe the charge on H2O?
polar
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why do H2O molecules have a polar charge?
hydrogen is slightly positively charged and oxygen is slightly negetivly charged (pulls electrons towards it)
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what are hydrogen bonds?
bonds formed between hydrogen and oxygen of dofferent H2O molecules, causing cohesion
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what happens to water above 100*C and why?
turns to gas as molecules have lots of energy and so hydrogen bonds are broken and molecules are free
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why is water liquid at room temperature?
molecules have enough energy to move around, forming and breaking hydrogen bonds as they do so
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why is water solid below 0*C?
there is not enogh energy for H2O molecules to move and break hydrogen bonds, so more hydrogen bonds are formed and water crystallizes
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why do some molecules (solutes) dissolve in water
if slightly charged, water molecules will cluster around it
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how many different R groups of amino acids are there?
20
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how do plants get amino acids?
yhey take nitrates from soil and use products o photosynthesis to make their own
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how do animals get amino acids?
eating protiens and digesting them (using protease) into amino acids, (some amino acids may be built by animals)
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what reaction is needed to turn amino acids into a Dipeptide?
condensation
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what reaction is needed to turn a dipeptide into amino acids?
hydrolosis
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what are the bonds between amino acids called
peptide bonds (covalent)
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what is the use of protease?
it breaks down peptide bonds between amino acids and this can be used in food digestions, hormone regulation (break down hormone), and helps to age skin (braks down collagen and protiens that make skin elastic and smoothe)
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what is the primary structure
a sequence of amino acids
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what is secondary structure of proteins?
hydrogen bonds form, creating alpha helix or a beta plated sheet
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in an alpha helix, how often are the hydrogen bonds?
every 4th amino acids
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how is tertiary structure formed?
alpha helix or beta plated sheet coil or fold to form 3D shape. this happens due to ionic, disulphide, hydrogen bnds and hydrophobic interactions between amino acids
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describe ionic bonds between amino acids
r groups wich are oppositely charged
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describe disulfide bonds/bridges between amino acids
if r groups contain sulpher, double bonds form between them s=s
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what are hydrophobic interactions in tertiary structure?
r groups wich are hydrophobic, will group together and exclude water from that area
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what is Quaternary structure?
a protien made up of more than one polypeptide or a polypeptide with an inorganic component.
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describe the structure of heamoglobin
globular protein, 4 polypeptide chains - 2 alpha chains and 2 beta chains. within each subunit ias a prosthetic group (ion Fe2+)
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describe the structure of collagen
fibrous protein made o 3 polypeptide chains twisted round eachother, each made of 100 amino acids, hydrogen bonds form between the chains, every 3rd amino acid is glycine (wich has only H as its R group)
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what is collagen fibril
collagen molecules heald together by cross links (covalent bonds)
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what is a colagen fibre
many fibrils held together
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what are the uses of collagen?
walls of arteries, skeletal muscle tendons, bones, cartilage and connective tissue
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what are monosaccharides
simple sugars (carbohydrate monomers)
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what are the properties of sugar?
sweet, soluble, form crystals
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what is the term for 3 carbon monosaccharides (each molecule has 3 carbon atoms)
Triose Sugars
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what is the term for 5 carbon monosaccharides (each molecule has 5 carbon atoms)
Pentose sugar
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what is the term for 6 carbon monosaccharides (each molecule has 6 carbon atoms)
Hexose sugars
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what type of monosacharide is glucose?
Hexose sugar
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what reaction is needed to turn 2 monosacharides into a disaccharide?
condensation
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what reaction is needed to turn a disacharide into monosaccharides?
hydrolysis
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what is the bond made in condensation reaction between glucose?
1-4 glycocidic bonds
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what is the name for the alpha glucose disaccharide?
maltose
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what does a chain of alpha glucose form?
straight chains of cellulose
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why is cellulose in strait lines?
every other beta glucose is inverted
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what are cellulose microfibrals?
chains of cellulose held together by hydrogen bonds
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what are cellulose macrofibrals?
microfibrals held together by hydrogen bonds
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how are cell walls formed
cellulose macrofibrals and pectins (polysaccharide glue)
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wich glucose can animal and plant enzymes break down for respiration
alpha glucose
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what is amylose?
lots of alpha glucose together to make a pring shape
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what are the properties of amylose?
compact, not water soluble and can trap iodine in it
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what is amylopectin?
similar to amylose chains, but have branches to allow easier access for enzymes
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what is starch?
a combination of amylopectin and amylose
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how are branches attached to alpha glucose chains?
1-6 glycosidic bond
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what is the difference between starch and glycogen?
glycogen has shorter 1-4 glycosidic bonds, and they have more branches, so it is more compact. also it is found in animal and starch is found in plants
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what are triglycerides?
a store of energy made of one glycerol and 3 fatty acids
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what reaction is needed to attach fatty acids to glycerol molecule?
condensation
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what is a fatty acid made of?
an acid and a hydrocarbon chain
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what are the components of a phospholipid
hydrophilic phosphate group, glycerol, and 2 fatty acids
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how are lipids respired?
hydrolisis of ester bonds
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what is the name of the bnd connecting fatty acids and glycerol?
ester bonds
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what gives out more energy lipid respiration or carbohydrate?
lipid
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what is the basic structure of cholesterol?
4 carbon based rings
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what is the test for protein?
add biuret to react with the peptide bonds and cause a colour change from blue to purple
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what is the test for reducing sugar (glucose)?
add Benedict reagent and heat at 80*C-90*C for 2mins and if present solution will go from blue to orange-red percipitate
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what is the test for non reducing sugars (sucrose)?
test for reducing sugars (make sure there is none there), boil with hydrochloric acid and turn sucrose into glucose and fructose then nutralise (using sodium carbonate) and now test for reducing sugar
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what is sucrose
glucose and fructose
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what is the test for starch?
add iodine (if present it will go from brown to deep blue/black)
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what is the test for lipids?
emulsion test. disolve in alcohol and add to water (go cloudy)
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Other cards in this set
Card 2
Front
define metabolism
Back
the sum of the total of all the chemical reactions that take place in an organism
Card 3
Front
Define organic chemistry
Back
Card 4
Front
why are covalent bonds strong and stable?
Back
Card 5
Front
define Monomer
Back
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