Which level of protein structure is disrupted through the hydrolysis of peptide
bonds?
Quaternary
Tertiary
Primary
Secondary - Primary
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.) - The original amino acid in a healthy patient is
glutamate, which is negatively charged. The mutated amino acid is valine, which isnon-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
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 - 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
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