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WGU C785 Biochemistry Unit Questions with Correct Answers

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WGU C785 Biochemistry Unit Questions with Correct Answers Which level of protein structure is disrupted through the hydrolysis of peptide bonds? Quaternary Tertiary Primary Secondary - Ans:-Primary ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 2...

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  • October 23, 2024
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  • WGU C785 Biochemistry
  • WGU C785 Biochemistry
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©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




WGU C785 Biochemistry Unit Questions
with Correct Answers

Which level of protein structure is disrupted through the hydrolysis of peptide bonds?




Quaternary




Tertiary




Primary




Secondary - Ans:✔✔-Primary




Page 1/58

, ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




The primary structure of a protein is the sequence of amino acids held together by peptide bonds.

Peptide bonds are formed by dehydration reactions and disrupted by hydrolysis.


A mutation in the beta-hemoglobin gene, which results in the replacement of the amino acid glutamate

in position 6 with the amino acid valine, leads to the development of sickle cell anemia. The structures of

glutamate and valine are shown below.




If the beta hemoglobin gene in a patient with sickle-cell anemia were to be edited so that the valine in

position 6 was replaced with a different amino acid, which replacement for valine would be expected to

have the best clinical outcome, in theory, for the patient? (Assume the valine can potentially be replaced

with any amino acid other than glutamate.) - Ans:✔✔-The original amino acid in a healthy patient is

glutamate, which is negatively charged. The mutated amino acid is valine, which is non-polar. Valine is

causing sickle cell anemia. The best amino acid to replace valine so that the patient is healthy again

would be the one most like glutamate, so any negatively charged amino acid.


Secondary, tertiary, and quaternary levels of protein structure can all be impacted by exposing a protein

to which treatment?




Change of a hydrophobic amino acid to a different hydrophobic amino acid




Page 2/58

, ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




Addition of a reducing agent




Placement of the protein in a solution with a low pH




Increase in the concentration of the protein in solution - Ans:✔✔-Placement of the protein in a solution

with a low pH




Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen bonds in the backbone of amino acids

occur in secondary structure, and both hydrogen bonds and ionic bonds occur in the side chains of

amino acids in tertiary structure.


An increase in beta-pleated sheet structure in some brain proteins can lead to an increase in amyloid

deposit formation, characteristic of some neurodegenerative diseases. What is the primary biochemical

process that follows the increase in beta-pleated sheet structure that leads to the development of the

amyloid deposits?




An increase in glycogen formation in the brain cells




Page 3/58

, ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




Aggregation of the proteins in the brain




Secretion of glucagon, leading to excessive ketogenesis




An increase in anaerobic metabolism of glucose in the brain - Ans:✔✔-Aggregation of the proteins in the

brain




This question is describing changes in protein structure. Aggregation occurs when proteins clump

together inappropriately, causing plaques like amyloid deposits to accumulate.


Which level of protein structure is determined by the sequence of amino acids?




Secondary structure




Quaternary structure




Page 4/58

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