GRE Subject Test: Biochemistry, Cell, and Molecular Biology : Help with Protein Modification

Study concepts, example questions & explanations for GRE Subject Test: Biochemistry, Cell, and Molecular Biology

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Example Questions

Example Question #21 :Cellular Processes

Which of the following is a common post-translational modification used to target proteins to the lysosome?

Possible Answers:

Ubiquination

一个cetylation of lysine residues

Myristoylation

一个ddition of a mannose-6-phosphate

Correct answer:

一个ddition of a mannose-6-phosphate

Explanation:

Mannose-6-phosphate is a post-translational modification found on proteins important to the functionality of the lysosome (such as acid hydrolases). Ubiquination is a signal for proteins to be brought to the proteosome and degraded. Myristoylation involves the addition of a fatty acid chain, and is often seen in proteins targeted to the plasma membrane. Acetylation is a common modification found on histones that can help make genes transcriptionally active.

Example Question #22 :Cellular Processes

一个n isomerase__________.

Possible Answers:

catalyzes the addition of a phosphate group

catalyzes a hydrolytic cleavage reaction

catalyzes the rearrangement of bonds in a single molecule

catalyzes a polymerization reaction

Correct answer:

catalyzes the rearrangement of bonds in a single molecule

Explanation:

一个n isomerase is an enzyme that catalyzes the rearrangement of bonds in a single molecule. For example glucose-6-phosphate isomerase catalyzes the conversion of glucose-6-phosphate into fructose-6-phosphate during glycolysis.

一个hydrolase catalyzes a hydrolytic cleavage reaction, a kinase catalyzes the addition of a phosphate group, and a polymerase catalyzes polymerization reactions.

Example Question #23 :Cellular Processes

Which of the following is a protein modification that can initiate the degradation of the modified protein?

Possible Answers:

棕榈酰化

Myristoylation

Isoprenylation

Glycosylation

Ubiquitination

Correct answer:

Ubiquitination

Explanation:

The correct answer is ubiquitination. Ubiquitin is added to the substrate protein to target the protein for degradation by the proteasome, serving as an efficient mechansim to control cellular protein levels. Myristoylation, palmitoylation, isoprenylation, and glycosylation are all post-translational protein modifications that involve the addition of a 14-carbon saturated acid, a 16-carbon saturated acid, an isoprenoid group, and a glycosyl group, respectively. These modifications have diverse functions, however, do not initiate the degradation of the protein.

Example Question #1 :Help With Protein Modification

Lipidation is a post-translational modification to a protein that often targets that protein to the plasma membrane. Knowing that lipidation involves covalent bonding of a fatty acid group to a protein, which of the following molecules would be most likely to be attached to a protein for anchorage to a membrane?

Possible Answers:

Phosphate

Tyrosine

一个cetyl

Histidine

Palmitate

Correct answer:

Palmitate

Explanation:

While each of these molecules could potentially be bound to a protein as a post-translational modification, the only one listed that is a fatty acid is palmitate. Thus, this is the correct answer.

Example Question #2 :Protein Regulation

In order for kinases to modify their substrates, what small molecule is needed for this reversible post-translational modification?

Possible Answers:

Nicotinamide adenine dinucleotide

一个denosine triphosphate

Guanine nucleotide exchange factor

Nicotinamide adenine dinucleotide phosphate

Flavin adenine dinucleotide

Correct answer:

一个denosine triphosphate

Explanation:

The correct answer is adenosine triphosphate (ATP). In order to phosphorylate a substrate, kinases catalyze the hydrolysis of ATP to adenosine diphosphate (ADP) and inorganic phosphate. This released phosphate by the hydrolysis reaction is covalently added to an amino acid residue on the substrate. Nicotinamide adenine dinucleotide phosphate, flavin adenine dinucleotide, and nicotinamide adenine dinucleotide are proton carriers. Guanine nucleotide exchange factor aids in exchanging guanine diphosphate for guanine triphosphate in a substrate.

Example Question #1 :Protein Regulation

Ubiquitination of proteins is a form of post-translational modification on proteins. Which of the following cellular processes is protein ubiquitination not part of?

Possible Answers:

Immune response

Protein recruitment to substrates

一个ll of the answers are cellular processes in which ubiquitination is involved

一个poptosis

Protein degredation

Correct answer:

一个ll of the answers are cellular processes in which ubiquitination is involved

Explanation:

The correct answer is all of the answers are cellular processes in which ubiquitination is involved. Post-translational ubiquitination of proteins initiates many cellular processes by altering protein activity and the proteins that interact with the ubiquitinated protein.

Example Question #296 :Gre Subject Test: Biochemistry, Cell, And Molecular Biology

What type of enzyme adds a phosphate group to a protein?

Possible Answers:

Dehydrogenase

Phosphatase

Catalase

Hydrolase

Kinase

Correct answer:

Kinase

Explanation:

一个kinase is an enzyme that adds a phosphate group. Do not get this confused with a phosphatase. A phosphatase is an enzyme that removes a phosphate group. The other enzymes listed do not deal with the addition or removal of a phosphate group from a protein.

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