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Principles > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

condensation

A

water removed

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2
Q

hydrolysis

A

water added

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3
Q

Oxidation

A

loss of electrons

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4
Q

reduction

A

gain of electrons

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5
Q

protein

A

chain of amino acid

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6
Q

peptide

A

chains of amino acids smaller than protein

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7
Q

lipids

A

fatty acids
soluble in inorganic substances but insouble in water
eg cholesterol

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8
Q

nucleic acid

A

composed of nucleotides

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9
Q

carbohydrates

A

composed of carbon, hydrogen and oxygen

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10
Q

efficiency of converting energy

A

energy cannot be created, only change form
converting energy from one source to another is not 100% efficient,and each time it occurs some of the energy becomes unusable
e.g. eventually there will be no usable energy

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11
Q

enthalpy

A

heat H

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12
Q

entropy

A

disorder S

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13
Q

change in free energy

A

ΔG° = ΔH° - TΔS°
temp in kelvin

ΔG° = energy of the products- energy of the reactants

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14
Q

free energy

A

the internal energy of a system minus the amount of energy that cannot be used to perform work.

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15
Q

exergonic reactions

A

ΔG° = -ve
the energy of the products is less than the energy of the reactants
can occur spontaneously

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16
Q

endergonic reactions

A

ΔG° = +ve
energy of the products is higher than the energy of the reactants
cannot occur spontaneously

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17
Q

what drives endergonic reactions

A

coupling to a exergonic reaction
many reactions coupled to ATP
ATP is highly unstable so produces energy by breaking 1 phosphate bond, stored as ADP

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18
Q

metabolism

A

all anabolic and catabolic reactions

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19
Q

catabolism

A

breaking down larger molecules to produce smaller ones
there are some energy consuming stages but net gain
exergonic and oxidative

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20
Q

anabolism

A

producing larger molecules from smaller molecules requiring ATP
endergonic and reductive

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21
Q

what is the ΔG of control reactions

A

large -ve ΔG° as the reaction will be mostly irreverisble as would require so much energy

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22
Q

water

A

polar, forms a dipole, ionic substances dissolve in water

non-polar substances are insoluble in water

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23
Q

amphiphilic

A

polar and non-polar

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24
Q

hydrophobic

A

water hating

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25
Q

hydrophilic

A

water loving

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26
Q

amino acids

A

form proteins
NH2, COO, H and side chain
amino group, carboxyl and H

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27
Q

categories of amino acid

A

acidic, basic, polar and non-polar

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28
Q

direction of amino acids

A

N terminus (amino group) to the C terminus (carboxyl terminus)

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29
Q

strength of peptides bond and the importance

A

strong, important for folding

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30
Q

acids

A

donate a proton( H+)
strength of an acid depends on how readily it donates the H+ e.g. strong acids will readily donate the H+ in water and fully ionise

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31
Q

Bases

A

Proton acceptors

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32
Q

pH

A

the concentration of H+ ions

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33
Q

buffer

A

solution to control the pH of a reaction mixture

resist pH change

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34
Q

proteins as buffers

A

proteins contain amino acid groups and carboxyl groups so are able to act as buffer
a change in pH can cause ionisation of proteins resulting in a change in protein structure and function

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35
Q

primary protein

A

sequence of amino acids

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36
Q

secondary protein

A

polypeptide backbone

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37
Q

tertiary protein

A

3D structure

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38
Q

quaternary protein

A

spatial arrangement of polypeptide chains with multiple subunits

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39
Q

Polypeptide rotation

A

polypeptides can rotate around the alpha carbon and the carboxyl group and they can rotate around the alpha carbon and the amino group.

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40
Q

bonds in secondary proteins

A

hydrogen bonds

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41
Q

3 types of secondary structure

A

1) alpha helix
2) beta pleated sheat
3) collagen triple helix

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42
Q

alpha helix

A

the H in the NH2 forms a bond with the O from C

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43
Q

B pleated sheet

A

zig zag

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44
Q

parallel B sheet

A

both strands start and end same place

e.g. both N-C or both C-N

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45
Q

antiparallel B sheet

A

the strands start and finish in different places eg one is C-N and the other is N-C

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46
Q

collagen triple helix

A

component of bone and connective tissue

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47
Q

bonds in primary protein structure

A

peptide

48
Q

tertiary proteins

A

fibrous and globular proteins

49
Q

bonds stabilising tertiary structure

A

ionic bonds
hydrophobic bonds
convalent disulphide bonds
hydrogen

50
Q

quaternary

A

proteins with more than 1 polypeptide chain

51
Q

transcription

A

RNA polymerase is used to transfer DNA to RNA

52
Q

translation

A

ribosomes translate the mRNA/RNA to an amino acid sequence

53
Q

nucleoside

A

base and sugar

54
Q

nucleotide

A

nucleoside and phosphate

55
Q

bonds between bases

A

AT is a double bond

CG is a triple bond

56
Q

DNA polymerase

A

synthesise DNA from deoxyribonucleotides

enzyme for DNA replication

57
Q

3’

A

has a free phosphate

58
Q

5’

A

has a free deoxyribose

59
Q

differences between DNA and RNA

A

RNA is single stranded while DNA is double stranded.
RNA has a sugar called ribose while DNA has a sugar called deoxyribose.
RNA has the base uracil while DNA has the base thymine.

60
Q

Replication

A

many sites of origin of DNA replication
nucleotides can only be added to the 3’ end
leading strand is continuous
lagging strand is added in short segments and joineed together by DNA ligase

61
Q

DNA ligase

A

joins together the okazaki fragments of the lagging strand

62
Q

chromosomes

A

carry DNA
one from mum and one from dad
23 pairs of chromosomes in each human cells

63
Q

rRNA

A

ribosomal ribonucleic acid

combines with proteins to form ribosomes where protein synthesis takes place

64
Q

types of rna

A

ribosonal rna
messenger RNA
transfer RNA

65
Q

mRNA

A

transfers a copy of the genetic code from the nucleus to ribosomes for protein synthesis

66
Q

tRNA

A

translates nucleotides to amino acids

67
Q

steps of transcription

A 
RNA polymerase binds
DNA sequence separates
Transcription is initiated 
Elongation: addition of further nucleotides 
Termination: release of finished RNA
68
Q

Types of mutation

A 
silent 
missense
nonsense
chromosomal 
frameshift 
point
69
Q

point mutation

A

change in a single base

70
Q

missense mutation

A

change in amino acid sequence and can change proteins function

71
Q

nonsense mutation

A

creates anew termination codon

72
Q

silent mutation

A

no chance on amino acid sequence

73
Q

frameshift mutation

A

insertion or deletion

74
Q

chromosomal mutation

A

large sections of the genome affected

75
Q

what happens to the finished protein

A

Tareted to location
modified
unwanted proteins are degraded

76
Q

factors

A

initiation, termination and elongation all require factors

77
Q

post translational modifications

A

glycosylation
disulphide bonds
cleavage

78
Q

Enzymes affect on equilibrum position

A

do not affect the equillibrum of reactions

79
Q

specificity

A

enzymes are v specific and stabilise the transition state

80
Q

how do enzymes reduce the actiation energy

A

provide an alternative pathway

81
Q

cofactors

A

assist enzymes

metal ions

82
Q

coenzymes

A

aid enzymes

organic molecules

83
Q

prosthetic group

A

tightly bought coenzymes

84
Q

haloenzymes

A

enzymes with cofactor

85
Q

apoenzyme

A

enzyme without cofactor

86
Q

isoenzymes

A

catalyse same reaction but different properties and structure

87
Q

phosphorylation

A

can activate or deactivate a protein

88
Q

irreversible convalent modifiation

A

activate of enzymes

eg digestive enzymes

89
Q

Vmax

A

Maximum velocity of a reaction ie inifinite substrate

the reaction velocity never reaches V max

90
Q

Km

A

substrate concentration that gives half of V max

91
Q

orthosteric inhibition

A

inhibitor binds at active site and blocks substrate acess

92
Q

allosteric inhibition

A

inhibitor binds at a site other than the active site and changes conformation

93
Q

irreversible inhibition

A

non-competitive, cannot be reversed, usually involves the formation or breakage of a convalent bond

94
Q

competitive inhibition on graph

A

Km varies but Vmax does not change

95
Q

non-competitive inhibition on graph

A

Km stays the same but Vmax changes

96
Q

allosteric enzymes

A

contain multiple subunits. binding of a substrate to one subunit causes a conformational change which causes a conformational change in the other subunits increasing their affinity for the substrate

97
Q

increasing substrate conc in allosteric enzymes

A

sigmoid curve

98
Q

what does a sigmoid curve show

A

cooperative behaviour

99
Q

what controls allosteric enzymes

A

allosteric inhibitors and allosteric activators

100
Q

glucose fermented

A

lactate

101
Q

glucose oxidised

A

pyruvate

ribose

102
Q

glucose stored

A

glycogen

103
Q

glucose transporters

A 
GLUT1: brain
GLUT2: liver
GLUT3:brain
GLUT4: muscles
GLUT5: gut
104
Q

where does glycolysis take place?

A

cyptoplasm

105
Q

hexokinase

A

regulates how much glucose is converted to glucose pyruvate

106
Q

phosphofructokinase

A

rate of flow

107
Q

pyruvate kinase

A

how much pyruvate leaves

108
Q

names of the control enzymes in glycolysis

A

hexokinase
phosphofructokinase
pyruvate kinase

109
Q

glycolysis activators

A

amp

fructose-2,6- biphosphate

110
Q

glycolysis inhibitors

A

ATP, citrate and H+

111
Q

where does the citric acid cycle take place

A

mitochondria

112
Q

orthosteric enzymes

A

bind to the active site

113
Q

isoenzymes

A

same function different structure

114
Q

kinases

A

phosphorylate

115
Q

zymogens

A

an inactive substance which is converted into an enzyme when activated by another enzyme

Principles (6 decks)

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