Abstract: Hydrophobicity manifests itself differently on large and small and length scales in physical and biomoleclar systems. We discuss the role of different length scale effects in protein folding and unfolding, the denaturing action of urea, and ligand binding to proteins.

Additional Information: Dr. Berne's lab's research focuses on understanding structural and dynamical processes in condensed matter and biophysical systems. Because they study many-body systems, it is necessary to utilize the powerful analytical methods of equilibrium and time-dependent quantum statistical mechanics as well as state-of-the art computer simulation methods such as molecular dynamics and quantum Monte-Carlo techniques. One important aspect of their research is the invention of new simulation. Recent work along these lines is their invention of a novel multiple time scale method in molecular dynamics and its application to the simulation of biomacromolecules, hydrophobicity, the detailed mechanism of chemical denaturation, and the effect of force on proteins. Another important activity involves the invention of new dynamical fluctuating charge force fields for complex molecular assemblies.

CSSB Distinguished Lecture Series: Fall 2010
10/12/2010 - Bruce Berne, Columbia University
10/26/2010 - Gary Siuzdak, The Scripps Research Institute
11/09/2010 - Charles Cantor, Boston University
11/11/2010 - Kristin Brown, GlaxoSmithKline
11/30/2010 - JoAnne Stubbe, MIT