Question

A group of Alzheimer's researchers noticed a particular protein isolated from patients has an abnormally high amount of beta-pleated sheet conformation. A new medication is now being engineered to alter the protein to a more alpha-helical structure. The conformation change is a result of altering which of the following?

A) Ionic interactions
B) Hydrophobic interactions
C) Hydrogen Bonds
D) Peptide Bonds
E) Disulfide Bonds

Answer 1

The transition from beta-pleated sheets to alpha-helices in protein structures involves the alteration of hydrogen bonds, which is the focus when engineering medication for Alzheimer's disease.

Step-by-step explanation:

The conformational change from beta-pleated sheets to a more alpha-helical structure in proteins, such as in the development of Alzheimer's therapy, primarily involves the alteration of hydrogen bonds. The alpha-helix and beta-pleated sheet are types of secondary structures in proteins held together by hydrogen bonds that form between the backbone atoms in the polypeptide chain. Altering these hydrogen bonds can lead to a change in the secondary structure of proteins, from a beta-pleated sheet to an alpha-helix, thereby potentially affecting the aggregation of amyloid proteins that is characteristic of Alzheimer's disease.