chapter 9 Flashcards

(53 cards)

1
Q

What is the Central Dogma of molecular biology?

A

DNA → RNA → Protein

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2
Q

What are proteins made of?

A

Proteins are polymers of amino acids.

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3
Q

What is the primary structure of a protein?

A

The linear sequence of amino acids in a polypeptide chain.

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4
Q

What are the two common secondary structures of proteins?

A
  • α-helix
  • β-pleated sheet
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5
Q

What defines tertiary structure in proteins?

A

The folding or interaction between secondary structures.

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6
Q

What is quaternary structure in proteins?

A

Proteins composed of multiple folded polypeptides joined by weak bonds.

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7
Q

What is the significance of protein shape?

A

Shape is essential to a protein’s function.

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8
Q

Name two types of protein shapes.

A
  • Globular proteins
  • Fibrous proteins
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9
Q

What is the role of transfer RNA (tRNA)?

A

tRNA translates codons into corresponding amino acids in a polypeptide.

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10
Q

What does the Wobble Hypothesis propose?

A

tRNA can recognize two codons due to flexible base pairing.

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11
Q

What is the genetic code described as?

A

Nonoverlapping and degenerate.

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12
Q

How many nucleotides are in a codon?

A

Three nucleotides.

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13
Q

What is a stop codon?

A

Codons that specify the end of translation.

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14
Q

What experiment helped crack the genetic code?

A

Making synthetic mRNA using polynucleotide phosphorylase.

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15
Q

What is the role of ribosomal RNA (rRNA) in ribosomes?

A

rRNA catalyzes peptide bond formation.

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16
Q

What is the function of aminoacyl-tRNA synthetases?

A

Attach amino acids to their corresponding tRNA.

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17
Q

What is the importance of the Shine-Dalgarno sequence in prokaryotes?

A

It helps position the initiator codon in the ribosomal P site.

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18
Q

What initiates translation in nearly all species?

A

Methionine specified by the codon AUG.

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19
Q

What is posttranslational processing?

A

Modifications after translation important for protein function.

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20
Q

What are the components of a ribosome?

A

One small subunit and one large subunit made of RNA and protein.

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21
Q

True or False: The genetic code is universal for all life.

A

True

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22
Q

Fill in the blank: The _______ is the region in the ribosome where peptide bonds are catalyzed.

A

Peptidyltransferase center

23
Q

What is the function of initiation factors IF1 and IF2 in bacterial translation?

A

They ensure that only the initiator tRNA enters the P site.

24
Q

In bacterial cells, what allows the initiation complex to form while another process is occurring?

A

Bacterial cells lack a nucleus.

25
What are the roles of eIF4A, B, and G in eukaryotic translation initiation?
They remove proteins and base pairings from mRNAs.
26
What is the first step in eukaryotic translation initiation?
Initiation factors associate with the 5’ mRNA cap, 40S subunit, and initiator tRNA to make the initiation complex.
27
How does the initiation complex in eukaryotes move?
It moves in a 5’ to 3’ manner and can unwind intramolecular base pairings.
28
What codon does the initiation complex scan for during translation initiation?
AUG codon.
29
What happens when the AUG codon is aligned with the initiator tRNA?
The 60S subunit joins to form the 80S ribosome.
30
What is the Kozak sequence?
The eukaryotic version of the Shine-Dalgarno sequence.
31
What starts the elongation phase of translation?
Initiator methionine in the P site.
32
What is the ternary complex in translation elongation?
EF-Tu, tRNA, and an amino acid.
33
What occurs when a correct tRNA matches with the mRNA codon?
The ribosome changes shape and ejects EF-Tu.
34
What happens in the peptidyltransferase center during elongation?
Peptide bond transfers methionine to the amino acid in the A site.
35
What does EF-G do during translation elongation?
Fits into the A site, causing tRNAs to move to P and E sites, and mRNA moves one codon through the ribosome.
36
What triggers the termination of translation?
The presence of one of the three stop codons (UGA, UAA, or UAG).
37
What are release factors?
Proteins that interact with stop codons and fit into the A site.
38
What is the role of water in the termination of translation?
It enters the peptidyltransferase center, causing the release of the polypeptide.
39
What is the definition of a genome?
An organism’s complete set of genetic material including all of the genes.
40
What is a proteome?
An organism’s complete set of proteins.
41
Why does the proteome produce more proteins than there are genes in the genome?
Due to alternative splicing and posttranslational modifications.
42
What are splice variants?
mRNA transcripts from the same gene but with different exon combinations.
43
What are isoforms?
Variant proteins produced from the same gene but from translation of splice variants.
44
What is the role of chaperones in protein folding?
They participate in the folding process to achieve the native form.
45
What are the two important types of chemical modifications that occur in proteins?
* Phosphorylation * Ubiquitination
46
What is the function of kinases?
Enzymes that add a phosphate group to specific serine, threonine, and tyrosine amino acids.
47
What do phosphatases do?
Remove phosphate groups from proteins.
48
What is the significance of protein-protein interactions?
They are central to the function of large biological machines such as the replisome, spliceosome, and ribosome.
49
What is ubiquitination?
The process that targets a protein for degradation by attaching ubiquitin.
50
What is the role of signal sequences in proteins?
They instruct proteins where to go, such as targeting them for secretion or embedding in the cell membrane.
51
What are nuclear localization sequences (NLSs)?
Amino acid sequences targeting proteins to the nucleus.
52
Fill in the blank: Most eukaryotic proteins are _______ unless modified after translation.
inactive
53
Fill in the blank: Posttranslational mechanisms recognize _______ in a protein sequence.
amino acid signatures