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biochemistry Flashcards

1
Q

name 2 polysaccharides

A

cellulose and glycogen

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2
Q

free energy chain equation

A

ΔG = ΔH – TΔS

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3
Q

exergonic reaction

A

total free energy of products < reactants

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4
Q

ΔG in exergonic reaction

A

negative

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5
Q

what reactions can occur spontaneously

A

exergonic

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6
Q

what is the net gain of ATP in glycolysis

A

2

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7
Q

how many ATP molecules are generated in glycolysis

A

4

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8
Q

what is Gluconeogenesis

A

Making new glucose from non-carbohydrate precursors, e.g. pyruvate

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9
Q

what reactions are used as control points

A

with large negative ΔG values

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10
Q

given an example of a catabolic pathway

A

glycolysis

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11
Q

give an example of an anabolic pathway

A

gluconeogenesis

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12
Q

what is stronger -H or covalent bonds

A

covalent

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13
Q

which amino acids is neither in D or L configuration

A

glycine

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14
Q

what are D and L forms

A

stereoisomers

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15
Q

describe peptide bonds

A

planar

partial double bond character

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16
Q

what does the HH equation do

A

calculate the properties of a buffer solution

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17
Q

what are zwitterions

A

amino acids without charged side groups

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18
Q

what is isoelectric pH

A

the pH at which a molecule has no net charge

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19
Q

given an example of a protein acting as a buffer

A

Hb in blood

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20
Q

what angles can the polypeptides rotate around

A

a carbon and amino group

a carbon and carboxyl group

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21
Q

what side is the a helix handed

A

right

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22
Q

what do proline residues do to a helix

A

break them

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23
Q

what are the turns between β sheets strands

A

glycine and proline

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24
Q

what protein has different 2y structure elements

A

phosphoglycerate kinase

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25
Q

what is tropocollagen

A

the molecular component of collagen

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26
Q

what does tropocollagen consist of

A

3 polypeptide chains coiled around eachother

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27
Q

what does covalent crosslinking in collagen do with age

A

inc

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28
Q

what does scurvy result in

A

weakened collagen - bleeding gums

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29
Q

fibrous proteins

A

contain polypeptide chains organised parallel long a single axis

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30
Q

fibrous protein exampple

A

keratin and collagen

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31
Q

globular proteins

A

spherical shape

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32
Q

globular proteins exmaples

A

myoglobin and Hb

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33
Q

name some forces stabilising 3y structures

A 
Covalent disulphide bonds
Electrostatic interactions = salt bridges
Hydrophobic interactions
Hydrogen bonds
Complex formation with metal ions
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34
Q

what does sickle cell anaemia result from

A

a change from glutamic acid to valine

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35
Q

what does sickle cell anaemia result in

A

rigid sickle shape cells - can block blood flow in capillaries

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36
Q

what results from incorrect protein folding

A

alzheimers, parkinsons, CJD

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37
Q

what is mad cow disease caused by

A

infection

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38
Q

what is CJD caused by

A

spontaneous or inherited mutation

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39
Q

what is CJD caused by

A

prion proteins

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40
Q

where are new nucleotides only added

A

to a free 3’ end

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41
Q

how many bonds between A and T

42
Q

how many bonds between C and G

43
Q

what is dna replication catalysed by

A

dna polymerase

44
Q

what are the properties of DNA polymerase

A

can only add to existing nucleic acids
can not start DNA synthesis on their own
require an RNA primer to start replication

45
Q

how is the lagging strand replicated

A

Okazaki fragments

46
Q

what unwinds teh DNA

47
Q

what is the RNA primer for DNA polymerase synthesized by

48
Q

what is the proofreading system that DNA polymerase has

A

3’ to 5’ exonuclease activity that removes incorrect nucleotides

49
Q

what does RNA contain

A

stem loops

50
Q

what does tRNA have

A

an anticodon

51
Q

what is the bonds that hold together primary protein structure

A

peptide (covalent)

52
Q

what does a-amanitin do to RNA polymerase II

A

inhibits it

53
Q

which type of RNA polymerase synthesises all mRNA

54
Q

how does transcription begin

A

binding of TFIID to TATA box

55
Q

what does TFIID

A

introduce kink into DNA and provide a landing platform fro further transciption factors and RNA polymerase

56
Q

does RNA polymerase require a primer

57
Q

what is the new RNA sequence to the template strand

A

complementary

58
Q

what is the new RNA to the coding strand

59
Q

how are steroids transported in blood

A

bound to albumin or other proteins

60
Q

what is added to the end of mRNAs

A

poly A tail and 5’cap

61
Q

how are free ribosomes translocated

A

post translationally

62
Q

how are bound ribosomes in RER translocated

A

co translationally

63
Q

how do enzymes reduce the activation energy

A

provide alternative pathways

64
Q

what is an apoenzyme

A

enzyme without a cofacotr

65
Q

what is a holoenzyme

A

enzyme with a cofactor

66
Q

what are tightly bound coenzymes called

A

prosthetic groups

67
Q

what are metalloproteins

A

Metal cofactors form a metal co-ordination centre in the enzyme

68
Q

what do vitamins function as

69
Q

what are isozymes

A

isoforms of enzymes that catalyse the same reaction but have different properties and structure

70
Q

what does lactate dehydrogasne do in the heart and muscle

A

H (Heart) – promotes aerobic metabolism

M (Muscle) promotes anaerobic metabolism

71
Q

what enzyme carries out phosphorylation reactions

72
Q

what are zymogens

A

inactive precursors of enzyme

73
Q

what is Km

A

half V max

74
Q

what is the intersection with x axis in Lineweaver-Burk plot

75
Q

what is the intersection with y axis in Lineweaver-Burk plot

76
Q

what has a higher affinity for glucose - hexokinase or glucokinase

A

hexokinase - lower Km

77
Q

what does a low Km suggest

A

high affinity of enzyme for its substrate

78
Q

do allosteric enzymes follow MM kinetics

A

no - sigmoidal curve

79
Q

where is GLUT3 found

80
Q

where is GLUT1 found

81
Q

what is glycolysis

A

conversion of glucose to pyruvate

82
Q

name 3 control points in glycolysis

A

hexokinase
Phosphofructokinase
pyruvate kinase

83
Q

what does hexokianse control

A

substrate entry

84
Q

what does Phosphofructokinase control

A

rate of flow

85
Q

what does pyruvate kinase control

A

product exit

86
Q

how is Phosphofructokinase controlled

A

energy change

87
Q

what is used to ferment pyruvate to lactic acid

88
Q

what is the Warburg effect

A

upregulation of anaerobic glycolysis in cancer cells - produce energy

89
Q

what must happen to NADH for glycolysis to continue

A

re oxidised - NAD+ is regenerated through the oxidative metabolism of pyruvate

90
Q

where does the TCA cycle occur

A

mitochondria

91
Q

TCA cycle - overall production

A

3 NADH
FADH2
2 CO2
GTP

92
Q

what is the enzyme of the TCA cycle that is not located in the mitochondrial matrix

A

succinate dehydrogenase - inner mitochondrial membrane

93
Q

what is the yield of one molecule of glucose

A 
4 ATP 
10 NADH 
10 H 
2 FADH2
4 CO2
94
Q

what does pyruvate dehydrogenase deficiency result in

A

poor muscle tone
retardation and seizures
resp problems

95
Q

where are ketone bodies formed

96
Q

are ketone bodies acid or alkali

A

strongly acidic

97
Q

what is diabetic ketoacidosis

A

Hyperventilation with a severe metabolic acidosis.

98
Q

what allows NADH from the cytoplasm to cross the inner mitocondrial membrane

A

malate aspartate shuttle

99
Q

what does a negative electron transport potential mean

A

reduced form of X has a lower affinity for electrons than H

100
Q

which resp complex doesn’t pump H

101
Q

what is ATP synthase also called

A

F1F0ATPase

102
Q

which part of ATP synthase protrudes into the mitochondiral matrix

RB Y1 Principles (16 decks)

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