Question

Proteins can be unfolded, or denatured, by agents that alter the balance of weak noncovalent forces that maintain the native conformation. How would the following agents cause a protein to denature? Be specific about the type of intermolecular forces that would be affected.

a) heat

b) pH

c) amphiphilic detergents

d) reducing agents such as 2-mercaptoethanol (HSCH₂CH₂OH)

Answer 1

a) Effect of heat:- when a protein is exposed to heat the kinetic energy of molecules is increased and thus molecules start vibrating thus breaks the hydrogen bonds and non polar hydrophobic interactions.

b) Effect of pH:- since their are ionic bonds present in the protein which are responsible in shape of protein when the pH is changed the ionic interaction undergo weakening and thus leads to the lose of these ionic bonds more over the hydrogen bonds are also disrupted by change in pH.

c) effect of amphiphilic detergents:- during the protein folding process the hydrophobic amino acids try to hide themselves which results in the hiding of the hydrophobic amino acids in the folded protein these interactions are called as hydrophobic interactions but once the detergents are added the hydrophobic interactions are disrupted leads to protein structure disruption.

d) Effect of beta mercaptoethanol:- these leads to the disrution of disulphide bonds present in between the sulphur containing amino acids.