Ken A. Dill, Ph.D.


We are interested in the physical properties of proteins. In particular, we are exploring: (1) the molecular forces that drive proteins to fold into their biological native structures, (2) how amino acid sequences encode those structures, (3) the thermodynamic factors that stabilize proteins against unfolding and aggregation, and (4) the rates and mechanisms by which proteins fold. We believe that knowledge of these physical properties can contribute to computer-based methods for predicting protein structures, dynamics, conformational changes, and their biological mechanisms.

We are also interested in the structure and physical properties of water. In particular, we have been developing simplified models that can be explored analytically and through Monte Carlo computer simulations, for the properties of pure water, for understanding hydrophobic interactions, and for ion solvation. We believe that better understanding of water as a solvent will have value in improving models in computational biology for the folding of proteins and RNA molecules and for ligand docking and drug design.

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