Unit 15- Proteins Flashcards

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1
Q

1 gene, 1 enzyme hypothesis

A
  • gene function by encoding enzymes, and each gene encodes a sep enzyme
  • aka 1 gene, 1 polypep hypothesis
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2
Q

Beadle and Tatum exper

A
  • isolated auxotrophic mutants in Neurospora
  • iradiated spores and placed on complete medium
  • moved to min medium where only auxotrophic survive
  • moved nonauxo to other mins w/ 1 amino acid. arginine was mutant as only place they survived
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3
Q

structure and function of proteins

A
  • proteins are polymers consisting of amino acids linked by peptide bonds
  • AA seq is primary structure
  • structure folds to create secondary and tertiary structures.
  • 2+ polypeptide chains associate to form quaternary structure.
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4
Q

dehydration reaction

A
  • removes H2O to form peptide bond between AA
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5
Q

codons

A

a triplet RNA code
- 64 possible codons
(3 stop and 61 sense codons)

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6
Q

degenerate code

A

AA may be specified by more than 1 codon

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7
Q

synonymous codons

A

codons that specify the same AA

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8
Q

isoaccepting tRNAs

A

diff tRNAs that accept the same AA but have diff anticodons

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9
Q

wobble hypothesis

A

base at 5’ end of tRNA anticodon can pair with several diff bases in a codon (only at 3rd base)

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10
Q

reading frame

A

way in which the seq can be read in groups of three. Each diff 3 part seq can encode a diff AA seq

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11
Q

nonoverlapping

A

a single nucleotide may not be included in more than 1 codon

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12
Q

translation of mRNA

A
  • Location: ribosome
  • N terminus: amino acid end at end of chain
  • C terminus: carboxyl end in the robosome
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13
Q

binding of AA to tRNA

A

Aminoacyl-tRNA synthetase: loads AA onto tRNA (tRNA charging)
- determines specificity between an AA and its tRNA
- 20 diff types (like 20 AA)

CCA: AA acceptor stem at 3’ end

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14
Q

initiation

A
  • initiation factor: IF-3 (and IF-2, and IF-1)
  • TRNA loaded with N-formylmethionine attached = fmet-tRNA
  • Energy molecule: GTP
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15
Q

initiation recognition seqs

A

The Shine-Dalgarno consensus seq in bacterial cells is recognized by the small unit of ribosome

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16
Q

steps of initiation

A
  1. If-3 binds to the small subunit
  2. small subunit binds to mRNA
  3. tRNA charged with N-forylmethionine forms a complex with F-2 and GTP
  4. bings to intiation codon and IF-1 joins small subunit
    5, initiation factors dissociate and GTP hydrolized to GDP
  5. large subunit binds
17
Q

elongation

A

-Elongation factors: Tu, Ts, G (EF-Tu; EF-Ts; EF-G)
- exit site = E
- Peptidyl site = P
- Aminoacyl site = A

18
Q

steps of elongation

A
  1. met tRNA in P site of ribosome
  2. EF-Tu, GTP, and charged tRNA form a complex and enter the A site
  3. GTP –> GDP and EF-Tu-GDP released (regenerates)
  4. peptide bond forms between AA and P site tRNA releases AA
  5. ribosome moves down mRNA and repeats
    (tRNA in P site now in E site and removed. tRNA in A site now in P site)
19
Q

Termination

A

release factors bind to termination codon, causing release of:
- peptide from last tRNA
- tRNA from ribosome
- mRNa from ribosome

20
Q

steps of termination

A
  1. reach stop codon
  2. RF-1 attatches to A site and RF-3 with GTP binds to ribosome
  3. everything released and GTP hydrolized
21
Q

polribosome

A

an mRNA with several ribosomes attached

22
Q

quality control

A
  • messenger RNA surveillance (detect and deal with errors in mRNA)
  • posstrnaslational modifications (folding: molec chaperones)
  • nonstandard AA synthesis