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
- C. C. Wan and J. Schofield, "Exact and asymptotic solutions of the mixed quantum-classical Liouville equation", J. Chem. Phys. 112, (2000) 4447-4459
- R. Iftimie and J. Schofield, "The separation of quantum and classical behavior in proton transfer reactions: Implications from studies of secondary kinetic isotope effects", Int. Journal of Quantum Chemistry 91 , 404-413 (2003)
- R. Iftimie and J. Schofield, "Reaction mechanism and isotope effects derived from centroid transition state theory in intra-molecular proton transfer reactions", J. Chem. Phys. 115, (2001) 5891-5902
- J. Schofield and M. Ratner, "Monte-Carlo Methods For Short Polypeptides", J. Chem. Phys. 109, (1998) 9177-9191
Created September 15, 1997. Last updated September, 2016.