Date of Award

4-20-2010

Degree Type

Thesis

Degree Name

Master of Science (MS)

Department

Chemistry

First Advisor

Dr. Donald Hamelberg - Committee Chair

Second Advisor

Dr. Davon Kennedy - Committee Member

Third Advisor

Dr. Stuart Allison - Committee Member

Abstract

Water is the most common solvent for most biological reactions, therefore it is vital that we fully understand water and all its properties. The complex hydrogen bonding network that water forms can influence protein-protein and protein-substrate interactions and can slow protein conformational shifts. Here, I examine an important property of water known as energetic roughness. The network of interactions between individual water molecules affect the energy landscape of proteins by altering the underlying energetic roughness. I have attributed this roughness to the making and breaking of hydrogen bonds as the network of hydrogen bonds constantly adopts new conformations. Through a novel computational approach I have analyzed five prominent water models and have determined their inherent roughness to be between 0.43 and 0.62 kcal/mol.

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