Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

[OS 201] 3rd Exam > Lippincott - Protein Synthesis > Flashcards

Lippincott - Protein Synthesis Flashcards

1
Q

direction of writing of codon

A

5’–>3’

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

number of base combinations

A

64

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

number of codons coding for amino acids

A

61

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

stop codons

A

UAA, UAG, UGA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

start codon

A

AUG

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

protein coded for by start codon

A

methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

characteristics of genetic code [4]

A

[1] specificity / unambiguity
[2] universality
[3] redundance / degeneracy
[4] nonoverlapping

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

specificity of genetic code

A

a particular codon codes for only one amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

universality of genetic code

A

genetic code found in all organisms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

redundance / degeneracy of genetic code

A

a single amino acid has more than 1 coding codon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

nonverlapping / commaless

A

code is read from a fixed starting point as a continuous sequence of bases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

consequences of altering nucleotide sequence [6]

A 
[1] silent mutation
[2] missense
[3] nonsense
[4] triple repeat expansion
[5] splice site mutation
[6] frameshift
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

silent mutation

A

single nucleotide mutation does not change the amino acid sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

missense

A

single nucleotide mutation changes amino acid sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

nonsense

A

single nucleotide mutation produces stop codon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

result of nonsense mutation

A

truncated protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

triple repeat expansion

A

amplification of a codon resulting in abnormally high amounts of a single amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

splice site mutations

A

failure to correctly splice the protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

frameshift mutation

A

addition or deletion causes change in reading frame and abnormal protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

how is amino acid linked to tRNA

A

carboxyl group of AA is in ester linkage with adenosine of CCA at 3’ end

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

anticodon

A

complement of codon in mRNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

codon

A

specifies amino acid needed for the sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

responsible for attachment of AA to tRNA

A

aminoacyl-tRNA synthetase

24
Q

mediators of circularization of mRNA preventing use of incompletely processed mRNA in translation

A

eIF-4 proteins, poly-A binding proteins

25
Q

where do eIF-4 proteins bind?

26
Q

prokaryotic ribosomal components

A

70S = 50S + 30S

27
Q

eukaryotic ribosomal components

A

80S = 60S + 40S

28
Q

[T\F] ribosomal proteins are more abundant in eukaryotic ribosomes

29
Q

products of RER ribosomes

A

proteins for export

30
Q

products of cytosolic ribosomes

A

proteins for the cell’s own use

31
Q

wobble hypothesis

A

movement of first anticodon base allows nontraditional pairing with 3rd base of codon, allowing tRNA to recognize more than 1 codon –> more flexible

32
Q

polycistronic synthesis

A

more than 1 coding region in mRNA

33
Q

monocistronic synthesis

A

only 1 coding region in mRNA

34
Q

type of coding in eukaryotes

A

monocistronic

35
Q

Shine-Dalgarno sequence

A

[1] purine rich sequence located upstream of AUG
[2] ribosome can recognize SD sequence
[3] binding or ribosome to SD sequence puts coding regions close to AUG

36
Q

direction of movement of ribosome along mRNA in translation

A

5’ –> 3’

37
Q

sites of ribosome

38
Q

ribosome - A site

A

A (aminoacyl) site; first binding site for charged tRNA - specifies the next amino acid to be added to the chain

39
Q

ribosome - P site

A

P (peptidyl) site; second binding site for charged tRNA - carries chain of amino acids that have already been synthesized

40
Q

ribosome - E site

A

E (exit) site; third binding site for charged tRNA - occupied by empty tRNA about to exit

41
Q

elongation in transcription

A

addition of amino acids to carboxyl end of growing chain

42
Q

elongation factors

A

mediate the delivery of aminoacyl-tRNA to the mRNA template in the A site

43
Q

responsible for catalysis of peptide bond

A

peptidyltransferase

44
Q

translocation

A

process by which the ribosome moves forward 3 nucleotides after creating a successful peptide bond

45
Q

enzyme required for translocation in eukaryotes

46
Q

release factor in eukaryotes

47
Q

polysomes

A

complex of 1 mRNA and a number of translating ribosomes

48
Q

important mechanism of translation regulation in eukaryotes

A

phosphorylation of eIF-2

49
Q

effect of eIF-2 phosphorylation

A

inactivation of protein, translation is not initiated

50
Q

cotranslational modification of protein

A

modification while protein is still attached to the ribosome

51
Q

posttranslational modification of protein

A

modification after synthesis has been completed

52
Q

trimming of proteins

A

proteins produced as large inactive complexes; cleavage/trimming is required to activate them

53
Q

examples of protein that uses trimming for regulation

A

inactive trypsinogen trimmed to become active trypsin

54
Q

covalent modifications that may activate or inactivate proteins [4]

A

[1] phosphorylation
[2] glycosylation
[3] hydroxylation
[4] carboxylation

55
Q

mechanisms of protein folding [2]

A

[1] spontaneous

[2] nonspontaneous (through chaperone)

56
Q

chaperone

A

protein that facilitates the proper folding of other proteins

[OS 201] 3rd Exam (10 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions