ribosomes and protein synthesis 2

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Last updated 11:57 AM on 10/7/26
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20 Terms

1
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what are eukaryotic tRNAs synthesised by?

RNA polymerase III

2
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what is splicing catalysed by?

endonucleases

3
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what are the 2 mechanisms in which editing is checked?

favourable binding

hydrolytic editing

4
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what is the favourable binding mechanism?

checking correct amino acid has the highest affinity for active side pocket of synthetase

5
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what is the hydolytic editing mechanism?

when tRNA binds, the synthetase tries to force adenylated amino acids into a second editing pocket

6
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what happens during elongation of the chain in protein synthesis?

peptide bond formation

large unit translocation

small subunit translocation

ribosome moves 3 nucleotides along

7
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which is the start coding sequence?

AUG

8
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what are the 3 stop codons?

UAA

UAG

UGA

9
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what happens at a stop codon?

release factors bind to the ribosome with the stop codon at the A site

this forces the peptidyl transferase to add a water molecule instead of aa

this frees the carboxyl end of the pp chain and the chain is released into the cytoplasm

10
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what is the structure of the proteosome?

central hollow cylinder

contains 6 subunit protein rings

11
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what are the most common modifications of proteins?

glycosylation

phosphorylation

12
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what is the function of chaperones?

help newly made or partly folded proteins to follow the right path, avoids mistakes

13
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what is the shape and functions of HSP 60?

barrel-shaped chamber

where proteins fold

14
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what is the function of HSP 70?

binds and stabilises growing or misfolded proteins

15
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why are some proteins eliminated?

misfolded or abnormal

damaged

alteration of cell state

16
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what are the general mechanisms for protein destruction?

activation of ubiquitin ligase

activation of degradation signal

creation of a ubiquitinylation site in response to intracellular or extracellular signals

17
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what is the carboxyl terminus?

a cleavage site where protease action removes the sequence after the protein is imported to the ER

18
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what do all signal sequences have?

10-15 hydrophobic amino acid residues

one or more positively charged residues

a short sequence at the carboxyl terminus

19
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what is N-linked glycosylation?

the attachment of an oligosaccharide to N

20
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where do modified proteins move to?

intracellular destinations