Bio Molecules

Monosaccarides into di
2 mono join through condensation reaction, OH + OH = H2O + glycosidic bond and visa versa
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Structure of starch
amylose = long, unbranched, alpha glucose, coiled, compact, good for storage. Amulopectin = long, branched, alpha glucose, side branches, easy for enzymes to break down
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Structure of Glycogen
polysaccharide of alpha glucose, similar to amylopectin
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Structure of Cellulose
long, unbranched, beta glucose, straight chains, linked layers of H bonds
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Structure of lipid
glycerol + 3x fatty acids (joined by ester bond)
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Tryglyceride
ester bond between each fatty acid + glycerol. formed by condensation reaction where water is relaesed. Synthesis of triglycerie = esterfication
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saturates vs unsaturated
saturated = no double bond in C atoms , unsaturated = at lease 1 double C bond
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Structure of amino acid
H2N -C-COOH ]R ]H
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Polypeptides
peptide bonds jon amino acids, make dipeptides and polypeptides
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Role of ionic, hydrogen and disulphide bonds
ionic= attraction between - and + R groups, hydrogen= waek bonds between + H and - H in R group Disulphide= surfur atoms join in amino acids
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Primary, secondary, tertiary and quaternery structure
primary= sequence of amino acids, secondary= H bonds between primary, make pleated sheet or helix, tertiary= coiled, more bonds formed quaternery= several polypeptide chains
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Collagen vs Haemoglobin
fibrous, strong molecule vs globular
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Structure of DNA
phosphate + pentose sugar + base, ester bond between phospahte and suger, H bond connecting molecules
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Semi-conservative replication
halicase breaks, single strand template for new, random bases in cell form new one, polymerase makes
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Gene
a sequence of DNA nucleotides that code for a protein (3 bases = 1 amino acid)
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RNA
AUGC, made in nucleus during protein synthesis, three adjustables babes = codon, carries genetic info
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structure of RNA
amino acid buliding site one end, sequance bases other end, carries amino acids used to make proteins
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Structure of enzymes
made of globular proetin, active site, induced fit= active site chnages shape a bit to fit substrate
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Enzyme as a catalyst
reduce activation energy
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Factors effecting rate of reaction in enzymes
temp= increase pH= 7 usually best optimum ph etc Concentration = more enzymes molecules=quicker
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Compeptive, non-compeptetive and end product inhibition in enzymes
competetive= similar shape to substrate to compete to get to enzyme, non-competetive= bind to enzym but not on actuve site
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Role of ions
nitrate= absorbed by plants in soil, calcium= holds cell walls magnesisum= makes chlorophyll phosphate= in photosynthesis and respiraton
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Importance of water as a dipole nature
slightly positive= charge of H attracts slightly, negative charge= of O makes water polar
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Properties of water
polar=attraction between molecules, cohesive, great for transporting substaces surface tension= cohesion, insects can glide
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Other cards in this set

Card 2

Front

Structure of starch

Back

amylose = long, unbranched, alpha glucose, coiled, compact, good for storage. Amulopectin = long, branched, alpha glucose, side branches, easy for enzymes to break down

Card 3

Front

Structure of Glycogen

Back

Preview of the front of card 3

Card 4

Front

Structure of Cellulose

Back

Preview of the front of card 4

Card 5

Front

Structure of lipid

Back

Preview of the front of card 5
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