Protein Structure Flashcards

(49 cards)

1
Q

What is the primary function of mRNA in protein synthesis?

A

It carries genetic information from DNA in the form of codons.

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2
Q

Which type of RNA is responsible for translating the mRNA code into an amino acid sequence?

A

tRNA (transfer RNA).

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3
Q

The binding of tRNA to mRNA is based on the complementarity between a codon on mRNA and an _____ on tRNA.

A

anticodon

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4
Q

What is the role of rRNA (ribosomal RNA)?

A

It associates with proteins to form ribosomes, which catalyze the assembly of protein chains.

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5
Q

Term: Translation

A

The processing of mRNA into a polypeptide or protein, mediated by ribosomes.

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6
Q

What are the fundamental building blocks that form protein polymers?

A

Amino acids.

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7
Q

What part of an amino acid determines properties like shape, charge, and hydrophilicity?

A

The amino acid side chain (R group).

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8
Q

What level of protein structure is represented by the linear sequence of amino acids?

A

Primary protein structure.

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9
Q

The alpha-helix and beta-pleated sheet are examples of what level of protein structure?

A

Secondary protein structure.

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10
Q

What type of bond is responsible for stabilizing secondary protein structures like the alpha-helix and beta-pleated sheet?

A

Hydrogen bonds.

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11
Q

The overall three-dimensional folding of a single polypeptide chain is known as its _____ structure.

A

tertiary

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12
Q

What level of protein structure involves the assembly of multiple polypeptide chains (subunits)?

A

Quaternary protein structure.

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13
Q

When does the folding of a protein’s N-terminal domain typically begin?

A

While the polypeptide chain is still growing and attached to the ribosome.

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14
Q

The process of modifying a protein after it has been synthesized is broadly known as _____.

A

post-translational modification

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15
Q

What is the term for the initial, unfolded polypeptide chain as it emerges from the ribosome?

A

Nascent polypeptide chain.

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16
Q

According to the diagram, what is the final step in forming a mature functional protein after folding, covalent modification, and cofactor binding?

A

Binding to other protein subunits.

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17
Q

Proteins destined for secretion or to be membrane-bound are synthesized by ribosomes associated with which organelle?

A

The endoplasmic reticulum (ER).

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18
Q

What is the term for the endoplasmic reticulum that is associated with ribosomes?

A

Rough ER (RER).

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19
Q

What type of sequence do proteins destined for the ER, organelles, or secretion typically contain at their N-terminus?

A

A signal sequence or signal peptide.

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20
Q

When protein transport into the ER occurs simultaneously with translation, this process is described as _____.

A

co-translational

21
Q

What is the simplest form of proteolytic cleavage that most proteins undergo after translation?

A

Removal of the first methionine residue.

22
Q

What is the primary function of phosphorylation as a post-translational modification?

A

To regulate the biological activity of a protein.

23
Q

Which type of enzyme transfers a phosphate group from ATP to a protein?

24
Q

Which type of enzyme removes phosphate groups from a protein?

A

A phosphatase.

25
Which three amino acids are typically subject to phosphorylation in animal cells?
Serine, threonine, and tyrosine.
26
The hydroxyl (-OH) group on serine, threonine, and tyrosine serves as the site for which type of modification?
Phosphorylation.
27
Sulfate modification of proteins occurs at _____ residues.
tyrosine
28
Unlike phosphorylation, sulfation is a permanent modification added for _____ and not for regulation.
biological activity
29
In most cases of acetylation, an acetyl group is added to which amino acid of a protein?
The N-terminal amino acid (after the first Met is removed).
30
What molecule serves as the acetyl donor for protein acetylation reactions?
Acetyl-CoA.
31
What is protein glycosylation?
The covalent linking of sugars to a protein.
32
What is the consensus amino acid sequence for the addition of sugars during glycosylation?
Asn – X – Ser/Thr.
33
Glycosylation serves as a major mechanism for what important cellular function?
Cell surface identification.
34
Post-translational methylation typically occurs at _____ residues in proteins like cytochrome c.
lysine
35
What molecule is the activated methyl donor for protein methylation?
S-adenosylmethionine.
36
The post-translational modification involving the addition of hydrophobic fatty acid chains for membrane anchoring is known as _____.
prenylation
37
Which vitamin acts as a required cofactor for modifications in proteins like collagens and peptide hormones?
Vitamin C (Ascorbic Acid).
38
Vitamin K serves as a cofactor in the carboxylation of _____ residues in certain proteins.
glutamine
39
The vitamin K-dependent carboxylation of glutamine allows a protein to chelate what type of ions?
Calcium ions.
40
What is the name of the small protein (8.5 kDa) that is covalently added to other proteins to regulate their stability and function?
Ubiquitin.
41
Ubiquitin is added to target proteins via which type of amino acid residue?
Lysine (Lys) residues.
42
What is the typical signal function of mono-ubiquitination?
It can be a signal for membrane transport or location.
43
What is the typical signal function of poly-ubiquitination?
It is a signal for proteolysis (protein degradation).
44
A protein that is tagged with a poly-ubiquitin chain is targeted for degradation by what cellular machine?
The proteasome.
45
Which type of enzyme transfers a phosphate group from an inorganic phosphate to a protein?
A phosphorylase.
46
Specific amino acid sequences in some proteins are recognized by _____ to promote rapid degradation.
peptidases
47
Prenylation involves adding compounds derived from the _____ biosynthetic pathway.
cholesterol
48
In the process of ubiquitination, what is the role of the E3 enzyme?
It recognizes the protein substrate and facilitates the transfer of ubiquitin to it.
49
During the final step of ubiquitination-mediated degradation, the proteasome breaks down the protein substrate into what?
Peptides.