Chapter 15 Flashcards

1
Q

one gene, ___ polypeptide

A

one

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2
Q

All enzymes are ___, but not all ___ are enzymes

A

proteins

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3
Q

What is an amino acid structure?

A

NH2-CHR-COOH

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4
Q

Define polar bonds.

A

covalent bond that shares electrons unequally

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5
Q

How are amino acids linked?

A

covalently by peptide bonds

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6
Q

What is are the phases of the protein structure?
Describe them.

A

primary:
- amino acid sequence

secondary:
- alpha helix or beta-pleated sheet
- peptide linkage and h-bonds

tertiary:
- polypeptide
- h-bonding, ionic bonding, s-s bonding (N-C), hydrophobic effect

quaternary (doesn’t always occur):
- protein
- polypeptide bonding

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7
Q

What are the types of stop codons?

A
  • UAA
  • UAG
  • UGA
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8
Q

What is the wobble effect?

A

3rd nucleotide of the codon can vary
- due to degeneracy of the genetic code

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9
Q

What is the name for the AUG codon?
- E. coli:
- Eukaryotes:

A
  • N-formylmethionine
  • methionine
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10
Q

What is tRNA charging?

A

the attachment of a tRNA to its appropriate amino acid
- to the 3’ OH
- ATP is required

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11
Q

Initiation: (translation)
What is the order of bind?

A
  • small ribosomal subunit to tRNA
  • initiation factors (proteins)
  • larger ribosomal subunit
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12
Q

How is translation/initiation different between E. coli and Eukaryotes?

A

E. coli:
- mRNA binds to sm subunit
- tRNA has N-formylmethionine

Eukaryote:
- mRNA is not directly involved
- start codons can be anywhere
- there can be more than 1 poly-cistronic mRNA
- tRNA has methionine
- GTP is used

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13
Q

Initiation: (translation)
Methionine is on the beginning of protein. What is this region call?

A

amino terminus (N-terminus)

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14
Q

Which direction is the protein formed?

A

n-terminus –> c-terminus

(amino) –> (carboxyl)

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15
Q

Elongation:
the Ribosomal small and large subunits share three sites to bind and interact with tRNA. What are they?

A

E: exit
P: peptidyl
A: aminoacyl

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16
Q

During transcription, does the mRNA move or remain bound to the tRNA?
Does the ribosome move?

A

mRNA remains bound to the tRNA, only the ribosome moves

17
Q

Transcription/Elongation:
The binding of new tRNA to the A site require what type of energy?

A

GTP

18
Q

How many base pairs does the ribosome move?

A

3 (1 codon)

19
Q

Transcription/Elongation:
When the ribosome moves, where does the amino acid of the tRNA, originally from the P site, transfer to?

A

to the amino acid on the new tRNA in the A site
- energy from amino acid-tRNA bond

20
Q

Transcription/Elongation:
What happens to the tRNA without an amino acid?

A

moves to the E site and diffuses away

21
Q

Transcription/Termination:
Are the stop codons bound to RNA? If not, what are they bound to?

A
  • no
  • release factors (proteins)
22
Q

Transcription:
How is elongation completed?
What energy type is used during this process?

A
  • the peptide is cleaved off of the last tRNA
  • whole complex falls apart
  • GTP
23
Q

Transcription/Termination:
What is the end of the peptide that was cleaved off of the last tRNA called?

A

carboxy terminus (C-terminus)

24
Q

What are polyribosomes?

A

each mRNA may be used by many ribosomes at once

25
Q

Transcription/Termination:
What aids in the folding of peptide?
What is removed during this process?

A
  • chaperone molecules
  • methionine
26
Q

Transcription/Termination:
What is usually cleaved off of the polypeptide?

A
  • longer sections at either ends
  • signal peptides
  • internal sections
27
Q

Transcription/Termination:
What may be chemically modified?

A

amino acids

28
Q

Transcription/Termination:
Is glycosylation rare in E. coli or animals?
What is it?

A
  • E. coli
  • attachment of s-s-s groups to proteins that are secreted/held on the outer surface of the cell membrane