biological molecules Flashcards

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1
Q

condensation reaction

A

when 2 monomers join and a water molecule is removed

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2
Q

hydrolysis

A

water molecules are added in the process of breaking down polymers into monomers

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3
Q

bond formed in condensation reaction

A

glycosidic

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4
Q

isomer

A

ions or molecules with identical formulae but different structures, not necessarily sharing the same properties

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5
Q

carbohydrate monomer

A

monosaccharide

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6
Q

carbohydrate polymer

A

polysaccharide

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7
Q

protein monomer

A

amino acid

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8
Q

protein polymer

A

polypeptide

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9
Q

nucleic acid monomer

A

nucleotides

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10
Q

nucleic acid polymer

A

ribonucleic acid / DNA

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11
Q

glucose + glucose =

A

maltose

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12
Q

glucose + fructose =

A

sucrose

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13
Q

glucose + galactose =

A

lactose

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14
Q

how is starch specialised for energy storage (5)

A
  • insoluble - doesn’t affect water potential/osmosis
  • large - doesn’t diffuse out of cells
  • compact - lots stored in a small space
  • forms α glucose which is easily transported and used in respiration
  • branched - has many ends which can be acted on by enzymes, releasing glucose monomers rapidly
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15
Q

glycogen found in…

A

animals and bacteria

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16
Q

structure of glycogen compared to starch

A

shorter chains, more highly branched

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17
Q

structural adaptations of glycogen (4)

A
  • insoluble - doesn’t affect osmosis/water potential
  • insoluble - doesn’t diffuse out of cells
  • compact
  • highly branched - increased enzyme activity = faster break down which is important to animals with a high metabolic rate
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18
Q

type of glucose glycogen and starch are made up of

A

α glucose

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19
Q

glucose type cellulose is made up of

A

β glucose

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20
Q

structure of cellulose

A

straight, unbranching chains, which run parallel to each other, with cross-linking hydrogen bonds between adjacent chains

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21
Q

function of hydrogen bonds in cellulose

A

adds strength to the molecule which provides rigidity for the plant

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22
Q

how is cellulose specialised for structural function (3)

A
  • molecules made up of β glucose = straight unbranching chains
  • collective strengthening effect of cross-linkage hydrogen bonds
  • molecules group to form microfibrils, which group to form fibres which add more strength
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23
Q

shared characteristics of lipids (4)

A
  • contain carbon, hydrogen, oxygen
  • proportion of oxygen to hydrogen and carbon is smaller then in carbohydrates
  • insoluble in water
  • soluble in organic solvents (eg. alcohols and acetone)
24
Q

main lipid groups

A

trigycerides (fats and oils)

phospholipids (main component of cell membrane)

25
Q

roles of lipids (5)

A
  • cell membrane - flexible, control transfer of lipid soluble substances across
  • source of energy
  • waterproofing - as insoluble in water
  • insulation - heat and electrical in myelin sheath around nerve cells
  • protection - stored after around delicate organs
26
Q

structure of triglycerides

A

3 fatty acids , 1 glycerol

27
Q

Test for non-reducing sugar

A
  • test for reducing sugar
  • add 2cm³ food sample to 2cm³ HCl
  • water bath for 5 mins (hydrolyse any disaccharides)
  • add sodium hydrocarbonate slowly (neutralise as Benedict’s doesnt work in acidic)
  • check alkaline using pH paper
  • retest with Benedict’s
28
Q

carbohydrate test

A
  • add 2 drops iodine into tube

- yellow -> blue/black if present

29
Q

pentose sugar

A

5 carbon atoms

30
Q

pentose sugars examples (2)

A

ribose

deoxyribose

31
Q

hexose sugar

A

6 carbon atoms

32
Q

starch made from

A
  • amylose

- amylopectin

33
Q

why is starch compact and insoluble?

A

because of the combined properties/structure of amylopectin and amylose

34
Q

structure of amylose

A

long straight chain that coils

35
Q

structure of amylopectin

A

long and branched

36
Q

why are triglycerides hydrophobic

A

they are non polar (there is no uneven distribution of charge within the molecule) meaning they don’t for hydrogen bonds with water molecules ∴ don’t dissolve in water

37
Q

general formula of a saturated fatty acid

A

CH3(CH2)nCOOH

38
Q

main lipid tests

A
  • sudan III
  • emulsion test
  • grease spot test
39
Q

emulsion test

A
  • 2cm³ into test tube containing 2cm³ absolute ethanol
  • dissolve by shaking vigorously
  • add equal volume of cold water
  • cloudy white suspension forms in presence of lipid
40
Q

sudan III test

A
  • 2cm³ sample to 2cm³ water
  • add a few drops of Sudan III and shake
  • red-stained oil layer separates on surface of water which remains uncoloured
41
Q

grease spot test

A
  • drop of sample on paper
  • allow to evaporate
  • permanent transparent spot on paper
42
Q

primary protein structure

A

specific sequence of amino acids in the protein joined by peptide bonds

43
Q

secondary protein structure

A

polypeptide chains fold into α helixor β pleated sheet - maintained by hydrogen bonds

44
Q

tertiary protein structure

A

protein folds up because various points on the secondary are attracted to one another - bonds = disulfide bridges, hydrogen bonds, ionic bonds

45
Q

quaternary protein structure

A

several units of tertiary bonds with H bonds and ionic bonds to form a functional protein, may also be prosthetic groups added

46
Q

prosthetic group

A

non-protein group

47
Q

properties/features of water (5)

A
  • cohesion - high surface tension which holds cells together
  • metabolite - in condensation, hydrolysis, photosynthesis and respiration reactions
  • a solvent - a medium for diffusion, allowing the transport of dissolved substances
  • high SHC - buffers change in temperature
  • high heat of vaporisation - provides cooling effect when evaporated (sweat) - large amount of heat lost with minimal water
48
Q

activation energy

A

the energy required to be supplied to the reactants to overcome their inter-molecular repulsive forces so that they can undergo a chemical reaction

49
Q

induced fit model of enzyme action

A

when the substrates combines with the enzyme and the enzyme changes shape, forcing the substrate molecules to combine/putting strain on the molecule, causing a particular bond to break - when substrate is released, enzyme returns to normal shape

50
Q

lock and key model of enzyme action

A

substrate drawn into a closely matching cleft on enzyme molecule

51
Q

competitive inhibitor

A

has a shape resembling shape of substrate - forms temporary enzyme-inhibitor complexes, blocking substrate

52
Q

non-competitive inhibitor

A

binds to enzyme at another site to the active site, changing tertiary structure, ∴ active site shape changes, ∴ no EZ complex’s made

53
Q

how does ATP release energy

A

hydrolysis of phosphate bond between 3rd and 2nd phosphate groups by ATP hydrolase - breaking bond releases energy

54
Q

limitations of lock and key model

A
  • assumes structure is rigid, which isn’t correct as observations show the activity of the enzyme can be altered by other molecules binding to it changing its shape ∴ structure = flexible
55
Q

effect of pH on enzyme activity

A
  • changes charges of amino acids in active site, meaning no E/Z complexes can be formed
  • if dramatic enough, may break bonds in tertiary structure, meaning active site shape changes
56
Q

describe protein structure [3]

A
  • polymer of amino acids
  • joined by peptide bonds
  • made in condensation reactions