The role of charge and aquation state plays an important role in the determination of macromolecular structure and chemical activity in biological systems. There has been very little theoretical work on how the conformation of an isolated macromolecule depends on the number of excess charges bound to it, in spite of the fact that many protein and polypeptide molecules contain ions and are present in a variety of charge states at biological pH conditions. We are working on new molecular dynamics and Monte-Carlo simulation methods which are designed to reproduce the correct statics and dynamics of charged polypeptides and other molecules in which proton transfer is important. The goal of the work is to probe how the transitions between folded and extended conformers depend on temperature, aqueous solvation and charge state of the molecule.

Relevant publications

This page is maintained by
Created September 15, 1997. Last updated September, 2016.