Chapter 6 Flashcards

1
Q

Translation

A

Production of polypeptides from mRNA

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2
Q

Building blocks of polypeptides

A

Amino acids

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3
Q

5 parts of amino acid

A
Central carbon
Amino group (NH3+)
Carboxyl group (COO-)
Hydrogen atom
R group (side chain)
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4
Q

What part of amino acid is “acid”?

A

Carboxyl group

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5
Q

Amino acids are joined by ____ bonds

A

Peptide

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6
Q

Ends of polypeptides

A
Free amino group (N terminus)
Carboxyl group (C terminus)
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7
Q

Which end of polypeptide is the beginning?

A

N terminus

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8
Q

Proteins shape determined by what two things?

A

Primary amino acid sequence

Cellular conditions that promote necessary folding

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9
Q

4 levels of protein organization

A

Primary
Secondar
Tertiary
Quaternary

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10
Q

Primary structure of proteins

A

Linear sequence of amino acids

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11
Q

Secondary structure of proteins

A

Shape taken by a polypeptide (or region of) by folding as a result of weak bonds like H-bond
Ex: alpha helix and beta sheet

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12
Q

Tertiary structure of proteins

A

3D shape of a polypeptide
Arises from folding of secondary structures
Can contain mixture of alpha helices and beta sheets

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13
Q

Quaternary structure of proteins

A

Only in multi-subunit proteins
Association of polypeptide chains
Ex: hemoglobin has 2 a and 2 b polypeptides

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14
Q

How many codons are there?

A

61 code for amino acids

3 code for stop

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15
Q

Is genetic code of amino acids universal?

A

Yes except for couple exceptions

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16
Q

Degeneracy of genetic code

A

Redundancy
More than one codon is used for each amino acid (except Met and Trp)
Allows wobble pairing

17
Q

tRNA

A

Transfer correct amino acids to codons
Single stranded
Each carries an anticodon and each can only attach to ONE kind of amino acid
Some tRNAs can recognize more than one codon

18
Q

Anticodon written from

A

3’ to 5’

19
Q

Wobble pairing

A

One anticodon can pair with more than one codon
3rd base of anticodon at 5’ end can wobble
This base not as constrained as 1st 2
Inosine can recognize A,U, and C

20
Q

Charging

A

Process of attaching correct amino acid to tRNA

Carboxyl group attached to 2’ or 3’ carbon

21
Q

Initiation of Translation in Prokaryotes

A

30S subunit and other IFs bind to ribosome-binding site aka Shine-Dalgarno sequence
tRNA fMet binds to AUG codon
50s subunit binds to 30s subunit

22
Q

Shine-Dalgarno sequence

A

Complementary to a sequence within the 16S rRNA of the 30S subunit

23
Q

fMet

A

tRNA attached to a modified form of methionine binds to AUG codon

24
Q

30S + 50S subunits=

A

70S initiation complex

25
70S initiation complex
Has 3 binding sites for tRNA | Prokaryotes
26
3 binding sites of 70s complex
Aminoacyl (A)- binds incoming aa-tRNA Peptidyl (P)- binds tRNA with growing peptide chain Exit (E)- contains uncharged tRNA to be released
27
Elongation of Translation in Prokaryotes
aa-tRNA binds to A site fMet is transferred from P site to aa in A site by ribozyme Translocation of ribosome to next codon Uncharged tRNA (w/o aa) is released from E site Process repeated until stop codon
28
Termination of translation in prokaryotes
Release factor protein binds to stop codon Triggers ribosome to cleave polypeptide from tRNA Components separate
29
Initiation of Translation in Eukaryotes
No shine-dalgarno sequence 40S ribosomal subunit binds to 5' cap and scans for Kozak sequence Once Kozak is found, 60S subunit binds to complex and AUG in Kozak is used for initiation
30
Simultaneous translations on mRNA in eu or prokaryote?
Both. | Average mRNA has 8-10 ribosomes at any time
31
Each ribosome translates how many amino acids per second?
15
32
Polysome
Complex between an mRNA and ribosomes