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Biochemistry > Protein synthesis > Flashcards

Protein synthesis Flashcards

1
Q

what are the folding problems

A

-systems at constant pressure and temp will seek equilibria

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2
Q

entropy of dentatured enzymes

A

high

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3
Q

entropy of native enzymes

A

low

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4
Q

define entropy with protein folding

A

the measure of conformation freedom

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5
Q

what is the flow of 1-4

A

1) assembly
2) folding
3) packing
4) interaction

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6
Q

describe binding sites

A
  • specific
  • chain needs to be 3D
  • forms ligands through non-covalent bonds
  • side chains form the site
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7
Q

what are the kinetics of folding

A

1) unfolded
- nucleation of folding-
2) I1 intermediate
- off path states Xn-
3) In molen globule
- final rearrangements;
4) folded protein

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8
Q

what are molecule chaperones

A

proteins an enzymes that bind to nascent and allows it to re-fold

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9
Q

why are molecular chaperones needed

A

help complete folding as the last folding requires a lot of energy

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10
Q

what do proteins want to be entropy

A

lowest entropy but still functional

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11
Q

what is the problem with protein folding

A

it happens in a high protein and amino conc environment so other reactions and folds can happen

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12
Q

what are hormones

A

substances that act on receptors to illicit a response

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13
Q

what does insulin do

A

stimulates glucose uptake and glycogen formation

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14
Q

what does insulin start

A
  • glucose uptake
  • glycolysis
  • glycogen synthesis
  • protein synthesis
  • uptake of ions
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15
Q

what does insulin stop

A
  • gluconeogenesis
  • glycogenesis
  • lipolysis
  • ketogenesis
  • proteolysis
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16
Q

what is an anabolic enzyme

A

build up

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17
Q

what are catabolic enzyme

A

break down

18
Q

why is insulin important

A

glucose wont enter cells without insulin

19
Q

what is the structure of insulin

A
  • 2 polypeptie chain w/ disulfide bridges

- dimeric

20
Q

where are disulfide bridged created

A

ER

21
Q

how is insulin synthesised

A
  • b cells in pancreas
  • 1 polypeptide composed of 3 chains is cleaved into 2 chains
  • released as heamer with 2 zinc ions in vesicle
22
Q

how is insulin produced from bacteris

A

Human pancreas cell

Remove DNA and specific insulin gene

Bacteria DNA plasmid –> remove plasmid

Bacteria plasmid + insulin gene = recombinant DNA

Introduce to bacteria

Fermentation

Bacteria secretes insulin

–> find a way to create disulfide bridges

–> yeast or mammalian cells

23
Q

what is fast acting insulin

A
  • injected at meal times
  • swapped proline and lysine at 28,29
  • takes less time to break down vessicle
24
Q

what is slow acting insulin

A

insulin that has 2 arginines and a glycine at the end

25
Q

what is the mechanism behind slow acting insulin

A

arginine shifts the isoelectric point to acidic to it is less soluble in physological
pH
glycine causes the hexamer to aggregate to a higher order

26
Q

what are structural genes

A

DNA regions that can be transcribed into proteins and RNA

27
Q

compare replication an transcription and how much genome

A

whole DNA genome is replicated but only some is transcribed

28
Q

what happens in transcription in prokaryotes

A

mRNA is used for translation without any processing

29
Q

what is an operon

A

a transcriptable region that contains several structural genes and upstream regulatory sequences

30
Q

what happens in transcription in Eukaryotes

A

1) DNA is exposed
2) coding happens from 3 to 5’
3) RNA polymerase created an mRNA molecule that is complementary to the DNA
4) pre-mRNA is spliced so intron are removed and exons are joined together
5) mature-mRNA leaves the nucleus

31
Q

what is RNA polymerase

A
  • 5 subunit enzyme
  • holoenzyme
  • -> apoenzyme +cofactor
32
Q

what do the sub units do in RNA polymerase

A

α =determines the DNA to be transcripted

β= catalyses polymerisation

β’ = bind + opens DNA template

δ = recognise the promoter for synthesis initiation

33
Q

what are codons

A

series of 3 non-overlapping nucleotides in mRNA

34
Q

what is the start codon

A

AUG

35
Q

what is the stop codon

A

UAA, UGA, UAG

36
Q

what are the 3 steps of translation

A

initiation
elongation
termination

37
Q

what happens in initiation

A

Start codon

MRNA moves into ribosome

TRNA with complimentary anticodon to the first codon moves into the ribosome

TRNA with specific anticodon is associate with an amino acid

MRNA attaches to TRNA

38
Q

what happens in elongation

A

Addition of other mRNA

MRNA shifts down the ribosome

Peptide bond forms between the amino acids via peptidyl transferase

First tRNA dissociates

39
Q

what happens in termination

A

Stop codon

TRNA releases polypeptide

TRNA leaves ribosome

40
Q

what does aminoacyl-tRNA synthase

A

attracts the appropriate amino acid to it tRNA

41
Q

what is the structure of tRNA

A

Clover leaf

Single stranded molecule with attachment site for amino acid

High energy bond

Opposite end has 3 nucleotide base called anticodon

42
Q

what are the 3 tRNA binding sites in ribosomes

A

A) aminoacyl-tRNA -> holds tRNA carrying next amino acid

P) peptidyl-tRNA -> holds tRNA attached to polypeptide chain

E) exit site

Biochemistry (10 decks)

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