Lecture 6 Flashcards

(35 cards)

1
Q

how many nucleotides are in a codon?

A

three

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2
Q

how many amino acids are there?

A

20

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2
Q

what is the concept of redundancy?

A

having multiple codons for one amino acid

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3
Q

what is the reading frame?

A

it is a way of dividing the nucleotides into sets of three

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4
Q

what is the mediator between mRNA and the protein sequence?

A

tRNA

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5
Q

how is redundancy managed? (2)

A

having more than one tRNA for the same amino acid

having tRNA that can base pair with more than one codon

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6
Q

where can ribosomes be found? (2)

A

on endoplasmic reticulum

in cytosol

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6
Q

what are ways of ensuring accuracy when matching with the genetic code? (3)

A

aminoacyl-tRNA synthetase

base pairing

aminoacyl tRNA synthetase correcting by hydrolytic editing

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7
Q

how is transfer RNA recognized? (3)

A

identifying the anticodon of the tRNA

recognizing the sequence on the acceptor’s arm

reading nucleotides on other positions on tRNA

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8
Q

How does the energy stored in the P site’s covalent bond between an amino acid and tRNA contribute to the energetically favourable peptide synthesis process?

A

makes peptide synthesis
energetically favourable

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9
Q

what is a ribozyme?

A

a ribosome with catalytic properties

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10
Q

what is the function of EF-Tu (EF1 in euk.)?

A

Checks
aminoacyl tRNA

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11
Q

what happens to EF-Tu if the base pairing is not correct?

A

not released

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12
Q

what happens to peptide bonds if the base pairing is not correct?

A

they will not form

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13
Q

what happens if the base pairing is correct? (2)

A

GTP is hydrolyzed

ET-Tu released

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14
Q

what is the purpose of the slight delay before the formation of p.p
bond?

A

allows one last check for accurate base-pairing

15
Q

what is the function of EF-G (EF2 in euk.)

A

helps the ribosome to move the mRNA
forward one codon at a time

helps speed up elongation of the
polypeptide chain

16
Q

Can ribosomes perform protein synthesis without the aid of elongation factors?

A

Yes, but…..slower and inefficient

17
Q

what is the role of elongation factors? (2)

A

improving speed and efficiency

error checking

18
Q

what is elongation mediated by?

A

GTP hydrolysis and release of EF-Tu & EF-G

19
Q

what does Polycistronic mean?

A

a type of mRNA molecule that carries the genetic information for multiple proteins

20
Q

what is the role of Shine-Dalgarno sequences during translation initiation in prokaryotes?

A

bind directly to the small ribosomal subunit’s mRNA-binding site.

21
Q

What is the significance of initiation factors (IFs) towards ribosomes during translation initiation?

A

IFs help position the small ribosomal subunit to the initiating AUG codon on mRNA

22
Q

During translation initiation, when does the large ribosomal subunit bind to the complex?

A

After initiation factors have dissociated

22
What is the typical spacing of nucleotides observed during protein synthesis?
Every 80 nucleotides
23
Which molecule binds to the initiator codon (AUG) during translation initiation?
Methionine tRNA
24
what is the function of the human translation release factor?
terminating translation by recognizing stop codons
25
Which are examples of molecular chaperones involved in protein folding?
Hsp60 and Hsp70
26
what is the function of chaperone proteins?
helps proteins fold
27
Which types of post-translational modifications are commonly observed in proteins?
Phosphorylation and glycosylation
28
What is the purpose of covalent modifications in proteins?
To make the protein active or to recruit it to the correct membrane or organelle
29
What is the cellular structure responsible for degrading proteins tagged with ubiquitin?
Proteasome
29
What cellular process targets proteins for degradation when they are tagged with ubiquitin?
Proteasomal degradation
30
Which enzymes are responsible for degrading proteins within the proteasome?
Proteases
30
what do many antibiotics act on?
ribosomes