1. Solvation and dynamics of chymotrypsin in hexane
- Author
-
Toba, S., Hartsough, David S., and Merz, Kenneth M., Jr.
- Subjects
Solvation -- Research ,Chymotrypsin -- Research ,Dynamics -- Observations ,Chemistry - Abstract
The solvent accessible surface area (SASA) of gamma-chymotrypsin (gamma-CT) decreases in hexane. The SASA increases for hydrophobic residues and decreases for hydrophilic residues. The spherical shape of gamma-CT is unchanged, and the protein shows no denaturation. The location of the essential water molecules and hydration affect its flexibility. Hexane is unable to solvate or diffuse into the core of gamma-CT. The net ion pair interactions and decreased ratio of the protein's surface area to volume stabilize gamma-CT in hexane.
- Published
- 1996