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My1 Principles > Biochem principles > Flashcards

Biochem principles Flashcards

1
Q

what is the strongest and weakest bonds

A

covalent –> hydrophobic interactions

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2
Q

when does REDOX and OILRIG mean

A

redox: when one thing is reduced another is oxidised.
OILRIG: oxidation is loss (of H), reduction is gain (of H)

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3
Q

what is the first law of thermodynamic

A

energy is neither created or destroyed

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4
Q

what is the 2nd law of thermodynamics

A

when energy is converted from one form to another some of it’s ability to do work is lost

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5
Q

what is free energy

A

a systems ability to ‘do work)

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6
Q

what is the equation for free energy

A

∆ = ∆H -T∆S

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7
Q

what is entropy

A

the amount of disorder within a system,

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8
Q

what is an exergonic reaction

A

free energy of the products is less than the reactants and so has a -ive value and can occur spontaneously

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9
Q

what is an endergonic reaction

A

when the total free energy of the products is more than the reactants and ∆G is +ive, this requires energy to proceed

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10
Q

if A + B –> C + D, what is the ∆G equation

A

∆G = ∆G + RTln([C][D]/[A][B])

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11
Q

what is the bodies preferred pH

A

pH 7

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12
Q

what does coupling of processes do to a endergonic reaction

A

coupling with a very -ive ∆G reaction to make an overall -∆G system

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13
Q

if ∆G is close to 0 what does this mean

A

can be easily reversed

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14
Q

what are the 4 types of amino acids

A

hydrophobic, polar, basic, acidic

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15
Q

what is at the N-terminal and is it +ive or -Ive

A

NH2, amino group, +ive

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16
Q

what is at the C-terminal ana is it +ive or -ive

A

COOH, -ive

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17
Q

what is an amino acid with no overall net charger

A

zwitterions

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18
Q

what is the difference between a acid and base

A

acids donate protons (H), and bases accept them

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19
Q

what is the pH equation

A

pH = -log10[H+]

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20
Q

what is the buffer equation

A

buffer = pka - log10[acid/base]

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21
Q

what is primary structure of an amino acid

A

chain amino acids are synthesised to

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22
Q

what is the secondary structure of amino acids

A

hydrogen bonds creating 3D structure: alpha helix beta sheets parallel or antiparallel

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23
Q

what is the tertiary structure for proteins

A

3D shape plus additional chains

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24
Q

what is the quaternary structure proteins

A

additional of subunits

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25
Q

what do chaperone proteins do

A

quicken protein folding

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26
Q

what can denature proteins

A

heat, extreme pH, detergents, reducing agents

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27
Q

what structure is triple helix

A

collagen

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28
Q

what is the central dogma

A

total DNA in genoma –> RNA –> protein

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29
Q

where does transcription occur

A

nucleus

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30
Q

where does transcription occur

A

nucleus

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31
Q

where does translation occur

A

cytoplasm

32
Q

what is a nucleoside

A

base and sugar

33
Q

what is a nucleotide

A

base and sugar and phosphate

34
Q

what connects at the 5’ end

A

phosphate

35
Q

what connects at the 3’ end

A

hydroxyl

36
Q

what direction does polymerase move in and what is required for synthesis

A

5’–>3’ and a primer

37
Q

what joins okazaki fragments on the lagging strand

A

ligase

38
Q

what unwinds DNA

A

helicase

39
Q

apart from synthesis DNA, what can polymerase do

A

remove incorrect DNA

40
Q

what are the differences between DNA and RNA

A

RNA has U not T, ribose not deoxyribose and is single stranded .

41
Q

what are the 3 types of RNA and what do they do

A

mRNA carries DNA replica to ribosome, tRNA carries amino acid to protein rRNA ribosomes

42
Q

what are promotors

A

specific nucleotide sequence to help initiate polymerase binding

43
Q

what is transcription elongation

A

transcription bubble moves along with polymerase, unwinding and rewinding

44
Q

what process removes introns and where does it take place

A

RNA splicing, nucleus

45
Q

what are degenerate amino acids

A

have multiple codons

46
Q

in initiation of translation what is required

A

GTP hydrolysation

47
Q

what site does a-tRNA originally bind to

A

A

48
Q

where does it move to when binding to other amino acids

A

P

49
Q

where does it leave from

A

E

50
Q

what does elongation factor (EF) do

A

brings a-tRNA to A site

51
Q

what enzyme catalysed peptide bonds between P and A amino acids

A

peptidyl transferase

52
Q

where are free ribosomes found

A

cytosol, nucleus, mitochondria

53
Q

where are bound ribosomes found

A

rough ER, golgi and membrane

54
Q

what can happen to amino acid chain after translation

A

post-translational modifications

55
Q

can enzymes change equilibrium

A

no but they change the rate it can be reached

56
Q

what do enzymes do to activation energy

A

lower it

57
Q

how do they do this

A

bind to transition state, stabilise it and provide alternative pathways

58
Q

what are cofactors

A

metal ions that assist enzymes

59
Q

what are coenzymes

A

organic molecules that assist enzymes

60
Q

what is an enzyme with a cofactor called

A

holoenzyme

61
Q

what is an enzyme without a cofactor called

A

apoenzyme

62
Q

what is an induced fit

A

when a substrate bind to active site it causes a conformational change making it fit better

63
Q

what are zymogens

A

inactive precursors of enzymes, irreversible reactions

64
Q

what is an isoenzyme

A

enzymes that catalyse same reaction but have different structures

65
Q

which enzymes phosphorylate

A

kinases

66
Q

what is vmax

A

max rate of reaction with unlimited substrate

67
Q

what is km

A

conc of substrate that gives 1/2 vmax

68
Q

in: E + S ES–> E + P. which reaction is K1, K2 and K-1

A

E + S –> ES = k1

E + S E + P = k2

69
Q

how do you calculate km or michalis constant

A

(k-1 + k2)/ k1

70
Q

what does a low km mean

A

low amount of substrate needed (high affinity)

71
Q

in a lineweaver burk plot, what shows Km and Vmax

A

y intercept = vmax

x intercept = Km

72
Q

do enzymes change vmax

A

no only km

73
Q

in competitive inhibition (orthosteric) of an enzyme, what happens to km and Vmax

A

Km increases and Vmax stays the same

74
Q

in non-competitive (allosteric) inhibition of an enzyme, what happens to km and Vmax

A

km stays the same and Vmax changes - binds to secondary binding site

75
Q

in orthosteric inhibition what does the curve look like, does it follow M-M rules

A

hyberbola, yes

76
Q

in allosteric inhibition what does the curve look like

A

sigmoid. no

77
Q

feedback control is what type of inhibition

A

allosteric

My1 Principles (12 decks)

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