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Biochemistry > Protein Synthesis > Flashcards

Protein Synthesis Flashcards

0
Q

Three letter code that specifies a particular amino acid; found within mRNA

A. Codon
B. Anti-codon
C. Amino acid

A

A. Codon

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1
Q

Complimentary code for a codon; found within a tRNA

A. Codon
B. Anti-codon
C. Amino acid

A

B. Anti codon

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2
Q

Differences more often than not lie within the last base

A

Wobble effect

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3
Q

True or false: multiple codons can code for a single amino acid

A

True; degenerate

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4
Q

True or false: single amino acid can be coded by multiple codons

A

True; degenerate

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5
Q

Particular codon can only code for a single amino acid

A. Degenerate
B. Unambiguous 
C. Non-overlapping
D. Unpunctuated
E. Universal
A

B.

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6
Q

Adapter molecule

A. mRNA
B. tRNA
C. rRNA

A

B. tRNA

cloverleaf shaped

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7
Q

Site of attachment for amino acid

A. Acceptor arm
B. D arm
C. Thymidine-pseudouridine cytidine arm
D. Anticodon arm

A

A. Acceptor arm

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8
Q

Recognition site for specific aminoacyl-tRNA synthetase; rich in dihydrouridine

A. Acceptor arm
B. D arm
C. Thymidine-pseudouridine cytidine arm
D. Anticodon arm

A

B. D arm

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9
Q

Binds aminoacyl tRNA to ribosomal subunit

A. Acceptor arm
B. D arm
C. Thymidine-pseudouridine cytidine arm
D. Anticodon arm

A

C.

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10
Q

Seven letter code containing the anticodon

A. Acceptor arm
B. D arm
C. Thymidine-pseudouridine cytidine arm
D. Anticodon arm

A

D. Anticodon arm

read in a 3’-5’ direction. The codon and anticodon are antiparallel with each other

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11
Q

Special enzyme that binds specific amino acids with their corresponding tRNAs, with the help of ATP

A

Aminoacyl-tRNA synthetases

Amino acids are attached via their carboxyl end at the 3’ end of the trna with an ESTER BOND, forming an aminoacyl tRNA

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12
Q

Initiation phase includes the following EXCEPT

A. Dissociation
B. 43S
C. 58S
D. 80S

A

C. It should be 48S

Dissociation includes 40 and 60S(eukaryotic)

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13
Q

Delays re association; allows for other IF’s to mingle with 40S

A. eIF-3, eIF-1A
B. eIF-2GTP
C. eIF-2
D. eIF-2GTP-met-tRNA

A

A.

Stabilizes the pre-initiation phase

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14
Q

43S preinitiation complex; initiation factor that binds to GTP

A. eIF-3, eIF-1A
B. eIF-2GTP
C. eIF-2
D. eIF-2GTP-met-tRNA

A

C.

eIF-2alpha phosphorylated in starvation states, preventing protein synthesis

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15
Q

Binds to met-tRNA

A. eIF-3, eIF-1A
B. eIF-2GTP
C. eIF-2
D. eIF-2GTP-met-tRNA

A

B.

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16
Q

Binds to 40S

A. eIF-3, eIF-1A
B. eIF-2GTP
C. eIF-2
D. eIF-2GTP-met-tRNA

A

D.

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17
Q

mRNA binds to 43S preinitiation complex via the methylguanosyl triphosphate cap

A. 43S preinitiation phase
B. 48S initiation complex
C. 80S initiation complex

A

B.

Uses up GTP; cap binding protein complex eIF-4F binds to the methyl cap (cap is only in eukaryotes)

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18
Q

A scaffolding protein

A. eIF-3, eIF-1A
B. eIF-2GTP
C. eIF-2
D. eIF-4G

A

D.

4G binds eIF-4E, eIF-3, eIF-4A/4B

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19
Q

Responsible for recognizing the mRNA cap; bound by BP-1 to inhibit initiation

A. eIF-3, eIF-1A
B. eIF-2GTP
C. eIF-2
D. eIF-4E

A

D.

Phosphorylated by insulin and mitogens to enhance initiation
mRNA cap region-rate limiting step in translation

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20
Q

Melts the secondary structure of the cap

A. eIF-3, eIF-1A
B. eIF-4A/4B
C. eIF-2
D. eIF-2GTP-met-tRNA

A

B.

Has ATPase-helicase activity

21
Q

48S initiation complex binds to 60 S subunit

A. 43S preinitiation complex
B. 48S initiation complex
C. 80S initiation complex

A

C.

eIF-5 hydrolyzes the GTP
All initiation factors are then removed

22
Q

elongation phase includes the following EXCEPT:

A. A-site attachment
B. Peptide bond formation
C. Degenerate
D. Translocation

A

C. Degenerate; not part, it is a characteristic of genetic code

23
Q

Elongation factor _________ complexes with GTP

A. eIF-1a
B. eEf-1a

A

B.

Seen in A-site attachment; complex binds with entering aminoacyl tRNA; charged aminoacyl tRNA then enters the A-site

24
Q

a-amino group of the A-site amino acid attacks the carboxyl end of te growing P-site polypeptide chain

A. A-site attachment
B. Peptide bond formation
C. Degenerate
D. Translocation

A

B.

25
Q

In peptide bond formation, it is facilitated by ________ a ribozyme component of the 60S subunit

A

Peptidyltransferase; ribozyme is an RNA with enzymatic properties; in this case, 28S RNA of the 60S subunit

26
Q

P-site tRNA os removed from the P-site

A. A-site attachment
B. Peptide bond formation
C. Degenerate
D. Translocation

A

D.

27
Q

Facilitates the transfer of A-site tRNA to the p-site

A

eEF-2

28
Q

Energy requirement for elongation phase

A

4 high energy phosphate bonds

Activation on tRNA- 2 ATPs
Entry of aminoacyl tRNA into A-site -1GTP
Translocation- 1GTP

29
Q

Where does stop codon enters

A. A-site
B. Peptide bond formation
C. Degenerate
D. Translocation

A

A.

30
Q

Remove the growing polypeptide from the P-site tRNA

A. eIF
B. eRF
C. eEF

A

B.

eRF-1 recognizes UAA, UAG
eRF-2 recognizes UAA, UGA
eRF-3 binds GTP

31
Q

Changes in the nucleotide sequence of a given DNA segment

A. mutation
B. Silence/nothing
C. Missense
D. Frameshift

A

A.

32
Q

Purine to purine OR pyrimidine to pyrimidine

A. Transition mutation
B. Transversion mutations

A

A.

33
Q

Purine to pyrimidine or pyrimidine to purine

A. Transition mutation
B. Transversion mutations

A

B.

In changing something, no frame-shift mutation occurs

34
Q

Type of mutation that is due to degeneracy of the genetic code

A. Nothing
B. Missense mutation
C. Nonsense mutation
D. Frameshift mutation

A

A.

35
Q

Amino acid that is replaced with another amino acid

A. Nothing
B. Missense mutation
C. Nonsense mutation
D. Frameshift mutation

A

B.

Results in acceptable, partially acceptable, or unacceptable results

36
Q

Codon coding for an amino acid is replaced with a stop codon

A. Nothing
B. Missense mutation
C. Nonsense mutation
D. Frameshift mutation

A

C.

Results in premature termination

37
Q

Error in reading the code due to either insertion or deletion

A. Nothing
B. Missense mutation
C. Nonsense mutation
D. Frameshift mutation

A

D.

38
Q

Hb A, beta chain and Hb S, beta chain; glutamine, valine

A. Acceptable
B. Partially acceptable
C. Unacceptable

A

B.

39
Q

Hb m (boston), alpha chain; tyrosine

A. Acceptable
B. Partially acceptable
C. Unacceptable

A

C.

40
Q

Protein synthesis change due to

A. Environmental threats
B. Viral infection
C. Both

A

C.

41
Q

Inactivates eEF-2

A. Ricin
B. Diptheria toxin
C. Aminoglycosides
D. Puromycin

A

B.

42
Q

Inactivates 28S rRNA

A. Ricin
B. Diptheria toxin
C. Aminoglycosides
D. Puromycin

A

A.

43
Q

A-site of ribosome; causes premature release of growing polypeptide

A. Ricin
B. Diptheria toxin
C. Aminoglycosides
D. Puromycin

A

D.

44
Q

Prevents initiation; 30S subunit

A. Ricin
B. Diptheria toxin
C. Aminoglycosides
D. Puromycin

A

C.

45
Q

Prevents binding of aminoacyl tRNAs to active site; 30S subunit

A. Ricin
B. Diptheria toxin
C. Aminoglycosides
D. Tetracyclin

A

D.

46
Q

Toxic molecule from castor bean

A

Ricin

47
Q

Acts as both prokaryotes / eukaryotes

A

Puromycin

48
Q

Inhibits peptidyltransferase; 50S subunit

A. Macrolides
B. Diptheria toxin
C. Chloramphenicol
D. Clindamycin/erythromycin

A

C.

Prokaryotes

49
Q

Inhibits translocation; 50S subunit

A. Ricin
B. Diptheria toxin
C. Clindamycin/erythromycin
D. Puromycin

A

C.

50
Q

Inhibits peptidyltransferase; 60S subunit

A. Cyclohexamide
B. Macrolides
C. Chloramphenicol

A

A.

Biochemistry (6 decks)

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