Question

What ultimately drives protein folding? What is meant by 'native state'? Denatured? Where would you expect to find the various classes of amino acids in a folded globular protein?

Answer 1

Protein folding is driven by hydrophobic and hydrophilic interactions. Hydrophobic amino acids are found in the interior, while hydrophilic amino acids are on the surface. Denaturation refers to the loss of a protein's structure, can be caused by extreme conditions, and may result in diseases.

Step-by-step explanation:

Protein folding is primarily driven by hydrophobic and hydrophilic interactions.

Hydrophobic amino acids tend to be found in the interior of a folded globular protein, while hydrophilic amino acids are typically found on the surface.

A protein embedded in a lipid bilayer, such as a plasma cell membrane, would have hydrophobic amino acids on the interior facing the lipid bilayer, and hydrophilic amino acids on the exterior facing the aqueous environment.

Denaturation refers to the loss of a protein's three-dimensional structure, which often leads to loss of function.

Denatured proteins can occur when proteins are exposed to extreme conditions like heat, pH changes, or exposure to chemicals.

An example of a disease caused by protein misfolding is Alzheimer's disease, where misfolding of the protein amyloid-beta leads to the formation of plaques in the brain.