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33 Cards in this Set
- Front
- Back
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function of buffers |
combine with/release H+ ions as required to shift pH (bicarbonate- blood) |
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cohesion adhesion |
cohesion: attraction btw same molecules adhesion: attraction btwn diff molecules (xylem) |
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organic compounds |
compounds containing carbon that are found in living organism |
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carb general formula and ratio |
CnH2nOn 2H:O |
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testing for glucose |
Benedicts reagent, produce brown precipitate on heating |
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bond formed between 2 monosaccharides |
1-4 glycosidic bond |
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testing for sucrose |
must be broken down first, then Benedicts reagent |
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benching chain bond |
1-6 glycosidic bond |
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test for starch |
iodine solution, turns blue-black |
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where is glycogen stored in body |
liver and muscles, but at night we use livers as have enzymes (breakdown of glycogen = LOTS of water) |
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lipids general formula |
CH3(CH2)nCOOH |
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how do lipids vary |
by fatty acid component (ALL GLYCEROL SAME) |
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why isn't lipid a polymer |
its a macromolecule only as can't join with other lipids |
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how do fatty acids vary |
- length of carbon chain - degree of saturation - location of double bond |
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function of lipids |
- energy store - provide insulation and reduce heat loss - structural component - provide waterproof quality (cuticle) |
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test for lipid |
produce red stain with Sudan III |
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steroid vs lipids |
has similar properties, diff structure |
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function of cholesterol in plasma membrane |
limits leakage improves permeability and fluidity |
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Cells only have C form amino acid. Who has D form? |
only few bacteria (mirror image of C) |
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what is amphoteric amino acids? |
behave as both acids and base |
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name for chains that contain few amino acids |
oligopeptides |
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where are peptide bonds formed in eukaryotic cells |
- cytoplasm - RER |
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what is the cause of secondary structures? |
hydrogen bonds between neighbouring CO and NH groups |
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what does disulphide bonds do |
give insoluble |
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reason for stability of alpha chain |
INTRA-chain H bond |
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beta pleated sheet characteristics |
- parallel pleat connected by H bonds (only INTER chain) H bonds - lack coiling ability - low extensibility - high strength and flexibility - eg: silk (fibroin) and spider web |
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what happens when alpha helixes combine? |
loses stretch characteristic (collagen) |
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what are the fibrous proteins? |
- myosin (for contraction) - fibrin (blood clotting) - collagen - keratin |
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why are globular proteins water soluble? |
- hydrophilic side facing out - surface of protein has many polar amino a. |
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what are heat shock/ chaperone proteins? |
- help other proteins fold correctly to get tertiary structure - can help denatured protein - prevent accumulation of useless protein, or else toxic (parkinson) |
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what are quartinary structure |
linkage of 2 or more polypeptide to form a single protein |
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conjugated protein |
made of amino acid chains and other NON protein (haemoglobin, glycoprotein) |
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what is proteome |
all the proteins encoded by the genome/ whole set produced by cell |
