Question

NMR studies on serine protease catalyzed reactions suggest that ________ observed between the catalytic Asp and His helps stabilize the transition state.

a) Ionic interactions
b) Hydrophobic interactions
c) Covalent bonds
d) Hydrogen bonds

Answer 1

Hydrogen bonds between the side chains of aspartic acid (Asp) and histidine (His) in serine proteases stabilize the transition state during enzyme catalysis.

Step-by-step explanation:

NMR studies on serine protease catalyzed reactions suggest that hydrogen bonds observed between the catalytic Asp and His helps stabilize the transition state. This stabilization is crucial for the proper functioning of the enzyme as it lowers the activation energy required for the reaction to occur. These hydrogen bonds form between a highly electronegative oxygen or a nitrogen atom and a hydrogen atom attached to another oxygen or nitrogen atom. In the context of serine protease, the hydrogen bond likely occurs between the side chains of the aspartic acid (Asp) and histidine (His), contributing to the catalytic mechanism of the enzyme.