WGU C785 Biochemistry Unit Exam Questions & Answers Latest 2021/2022

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Answers Latest 2021/2022 1. Which level of protein structure is disrupted through the hydrolysis ofpeptide bonds? Quaternary Tertiary Primary Secondary: Primary The primary structure of a ... protein is the sequence of amino acids held together bypeptide bonds. Peptide bonds are formed by dehydration reactions and disruptedby hydrolysis. 2. A mutation in the beta-hemoglobin gene, which results in the replacementof 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 clin-ical outcome, in theory, for the patient? (Assume the valine can potentially be replaced with any amino acid other than glutamate.): 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. Thebest amino acid to replace valine so that the patient is healthy again would be theone most like glutamate, so any negatively charged amino acid. 3. Secondary, tertiary, and quaternary levels of protein structure can all beimpacted by exposing a protein to which treatment? Change of a hydrophobic amino acid to a different hydrophobic amino acidAddition of a reducing agent Placement of the protein in a solution with a low pH Increase in the concentration of the protein in solution: Placement of the 1 / 27 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. 4. An increase in beta-pleated sheet structure in some brain proteins can [Show More]

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