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biochemistry Flashcards

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1
Q

what is the other name for proteins? and what does this mean?

A

polypeptides- many amino acids

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2
Q

how many amino acids do we have?

A

20

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3
Q

how many essential amino acids and what does this mean?

A

9 essential- need to eat, we cannot make

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4
Q

ow many non-essential amino acids and what does this mean?

A

11 non-essential- body makes

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5
Q

how are amino acids joined?

A

by a condensation polymerisation reaction which forms a repeating backbone with alternating R groups.

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6
Q

chirality?

A

amino acids have a chiral carbon centre which means that the have 4 different environments all around- an amine, R, H, carboxy

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7
Q

what are the exceptions in amino acids?

A

glycine is not chiral

proline changes from the general structure (but still chiral)n

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8
Q

what is the basic end? acidic end?

A
  • amine

- carboxy

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9
Q

how are amino acids categorised?

A

by the properties of the R group

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10
Q

non-polar

A

dispersion forces only

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11
Q

+ charge

A

has an NH3+, NH2+ or NH+

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12
Q

polar

A

has an OH, C=O

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13
Q
  • charge
A

lost some H forming O-

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14
Q

what does it mean that amino acids can acid as buffers?

A

they have amphiprotic capacity- act as an acid or base, this leads to conjugate pairs

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15
Q

what aspects does a zwitterion have?

A

a positive (protonated) and negative (deprotinated) end

  • neutral overall
  • protonated end is basic and accepts H+ in acidic solutions
  • deprotinated end is acidic and donates H+ in basic solutions
  • therefore amphiprotic and acts as a buffer
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16
Q

important note in buffering?

A

R groups can participate

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17
Q

at pH 7?

A

always zwitterions because neutral

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18
Q

how are dipeptides formed?

A

water is expelled, allowing C=ONH (amide link or peptide link) to form

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19
Q

what if dipeptides are being broken down?

A

add water ands its hydrolysis

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20
Q

number of waters lost?

A

number of amino acids-1

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21
Q

working out number of possibilities

A

use factorials

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22
Q

how does hydrolysis work?

A

water is added, the amide link breaks

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23
Q

primary structure

A

bead chain of amino acids

- peptide bonds (covalent bonds)

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24
Q

secondary structure

A

hydrogen bonding occurs causing folding on b-sheet or a-helix

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25
Q

tertiary structure

A
  • 4 different types of bonds (governed by R groups)
  • dispersion
  • ionic (charges)
  • hydrogen
  • disulphide (S-S)
    order of strength
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26
Q

quaternary structure

A
  • when more than one pp chain join together eg. ribosomes, antibodies, haemoglobin
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27
Q

protein function

A 
structure- keratin 
transport- Hb
toxins 
defence, immunology- antibodies 
enzymes- biological catalysts
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28
Q

what are enzymes and what do they do?

A

speed up reactions by lowering activation energy needed to break reactant bonds. this leads to energy conservation (more energy put into increasing collisions) and therefore ensures another energy pathway to be present

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29
Q

what does it mean that enzymes are specific?

A

an enzyme only functions on a specific substrate. this is linked to their 3D structure and active site (Complementary bonding)

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30
Q

how does the lock and key model work?

A

when the substrate (key) internal bonds releax, the activation energy is decreased and therefore bonds break more easily

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31
Q

enzymes can be reused

A

they are not consumed by a reaction

32
Q

enzyme-substrate complex

A

when lock and key fuse

33
Q

induced fit model

A

active site is modified to better fit the substrate

34
Q

what are the set conditions under which enzymes function?

A

optimal conditions- pH and temperature

changes to these change bond types and disrupt 3D structure

35
Q

less than optimum temperature

A

decrease kinetic energy, do not denature (not enough energy)

- hypothermia

36
Q

greater than optimum temperature

A

denature, 3D structure destroyed, R groups cannot bind, pp chain undone, coagulation (clump)
- hyperthermia

37
Q

what are coenzymes formed from?

A

vitamins we eat

38
Q

what do many coenzymes work?

A

with a cofactor

39
Q

what are cofactors?

A

metal ions (cations) or small organic molecules (not proteins)

40
Q

what is 1 coenzyme function?

A

attach functional groups to the substrate- phosphorylation or methylation
- cofactor, coenzyme and substrate bind and coenzyme passed functional group onto the substrate

41
Q

what is 2 coenzyme function?

A

carry electrons

  • oxidation and reduction
  • NAD+ and H+ and 2e- form NADH
  • same with FAD+
  • NAD and FAD are both oxidants
42
Q

how does a coenzyme differ to an enzyme?

A

a coenzyme needs a cofactor to function

43
Q

how does a cofactor work?

A

the coenzyme is inactive but when a cofactor binds, it becomes activated and can then bind to the substrate

44
Q

what are carbohydrates made of?

A

CHO

45
Q

what is the equation of carbohydrates?

A

Cx(H2O)y where x and y are equal

46
Q

what are carbohydrates a source of?

A

energy

47
Q

what are the three groups of carbohydrates?

A
  • monosaccharides
  • disaccharides
  • polysaccharides
48
Q

what are monosaccharides?

A
  • one sugar
  • simple sugars
  • glucose, galactose, fructose

glucose and galactose are isomers and hexose

fructose is pentose

they are highly soluble due to hydrogen bonding

49
Q

what are disaccharides?

A
  • 2 sugars added together
  • condensation reaction
  • bind 1 to 4 (horizontal) and water is expelled
50
Q

what are polysaccharides? what are the types?

A
  • many sugars
  • continued condensation reactions
  • starch, cellulose, glycogen
51
Q

what is starch? what are the types? how does bonding occur? solubility?

A

polymer of glucose, stored in plants in the leaves and seeds

amylopectin- soluble in water due to its branching structure which exposes OH
- has bonding 1 to 4 horizontal and 1 to 6 vertical

amylose- insoluble in water as OH are not exposed
- only 1 to 4 bonding

52
Q

what is cellulose? humans? bundle parallel?

A

polymer of beta glucose (humans have alpha). The humans don’t have enzymes to break it down, fibre

have 1 to 4 bonding and 1 to 6 bonding to form parallel lines

53
Q

what is glycogen? bonding?

A

a polymer of glucose. it is in excess in humans in liver and muscle cells

mainly 1 to 4 bonding (glycosidic linkage) but also some branching with 1 to 6 glycosidic links

54
Q

what are glycosidic links?

A

C-O-C also called ether links and can be 1 to 4 or 1 to 6

55
Q

how does hydrolysis of sugars occur?

A

water is added and an enzyme breaks glycosidic link

56
Q

what is GI?

A
  • glycemic index
  • a way of rating CHO food
  • rates on affect on Blood Glucose Level over a period of time, namely 2 hours
  • rates food on how quickly it releases the energy it contains
57
Q

low GI

A

long time to release energy

58
Q

what is biological availability?

A

how readily available the energy is in the food we eat

59
Q

what are lipids?

A

fats

- ester

60
Q

what are triglycerides?

A

3 glycerol fatty acids (carboxylic acids)

61
Q

how do glycerols and fatty acids form to made a triglyceride?

A

glycerol and three fatty acids join by condensation reactions, expelling 3 waters and creating an ester link

62
Q

how are triglycerides broken down?

A

add water

63
Q

polarity of fatty acids? implications?

A

long hydrocarbon chains that are non-polar. therefore when moving in the blood stream, the lipids need the help of bile

64
Q

what is bile?

A

a lipoprotein that is a surfactant- chemical that has a non polar nd and a polar end
looks like a circle (polar) with a zig zag end (non-polar)

65
Q

how does the fatty acid travel with bile?

A

in the middle with the polar circles pointing out as they travel through the polar environment

66
Q

what are the physical states of lipids?

A

solid- butter, lard, wax

liquid- oil

67
Q

what are the chemical structures of lipids?

A
  • saturated: no C=C bond, ane
  • unsaturated: C=C bond, ene
    can be polyunsaturated or monounsaturated
68
Q

what do saturated and unsaturated fatty acids look like?

A

saturated are straight

unsaturated have a kink

69
Q

comparing butter and oil?

A

butter is saturated and therefore has a higher boiling point because with no C=C there are lots of H to engage in dispersion forces and therefore more intermolecular bonding and more energy to overcome

oil is unsaturated and has a lower BP. this is because of less H atoms to dispersion force because of double bonds. therefore less energy to overcome and therefore less heat needed to overcome

70
Q

what is the general structure of fatty acids?

A

alpha end COOH and omega end CH3

71
Q

how do you determine whether a fatty acid is unsaturated and how many C=C bonds it has?

A

ignore COOH
subtract CH3
use CxH2x formula
if number of hydrogens is not equal, it is unsaturated
subtract hydrogens present from those of CxH2x
divide that number by 2 which will give the number of C=C bond

72
Q

what is a cis-fatty acid?

A

Hs on the same side of the C=C bond and therefore chain has a large kink

73
Q

trans-fatty acid?

A

Hs are on opposite sides of the C=C bond and there is a smaller kink due to this, they can stack which causes health issues

74
Q

omega 3 fatty acids?

A

first double bond is on the 3rd carbon from the end

75
Q

omega 6 fatty acid?

A

the first double bond is on the 6th carbon from the end

Chemistry (28 decks)

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