Proteins are dynamically active assemblies. Emerging evidence continues to suggest existence of thermodynamical coupling between hydration shell and bulk solvent, and the protein internal motions. Our combined experimental-computational investigations indicate close interconnection between the fluctuations of the solvent on the protein surface. This close coupling plays a role in driving protein conformational changes, which in turn impact the designated function of protein such as enzyme catalysis. We are currently performing investigations of enzyme catalysis in mixed organic solvents that provide a mechanism for controlling the interaction between solvent and enzyme surface. Detailed results from neutron scattering, X-ray crystallography and computational studies will be presented for enzyme dihydrofolate reductase.

Unraveling the mystery of solvent-protein thermodynamical coupling: Insights from enzyme catalysis in organic solvents

244th National Meeting (2012)

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