Huan-Xiang Zhou | Homepage
Professor of Physics
Interactions of proteins among themselves and with other molecules such as DNA, RNA, and membranes are essential for biological functions. Our research aims to gain fundamental understanding of the determinants of binding affinity and binding rates. Based on statistical mechanics, we develop physical models that can be implemented on the computer to realistically predict binding properties.
The folding of a protein molecule can be viewed as the accumulation of native contacts. Based on modeling the unfolded protein molecule as a polymer chain, we have developed a theory for the rate of forming native contacts. This theory is now being extended and applied to study folding processes such as beta-hairpin and coiled-coil formation. In addition, molecular dynamics simulations of protein unfolding are carried out to elucidate the transition state of folding.
The major stabilizing forces of protein structures are hydrophobic and electrostatic. While there is consensus on the hydrophobic contributions, the roles of electrostatic interactions in protein stability have been uncertain. We have made significant progress in modeling electrostatic effects. We are now developing better solvation models using as benchmarks experimental data and molecular dynamics simulations with explicit solvent and investigating effects of charges and electrostatic interactions in protein folding, binding, aggregation, and amyloid formation.