Abstract: The reversible, specific binding of proteins is an essential element in most biological processes. Understanding how proteins interact with each other to form stable complexes is therefore a necessary step in understanding many cellular processes such as signal transduction, antigen-antibody recognition, and regulation of gene expression. A molecular insight into the binding specificity in protein-protein complex is also useful for the design of potent and specific protease inhibitors with therapeutic value. Here we report the results of computational docking and binding free energy calculation on a series of protein-protein complexes. We use molecular dynamics simulation to investigate quantitatively the interaction between protein binding partners. We also analyze the computational protein docking results to obtain qualitative pictures of binding.

Summary of qualifications：Computational chemist with background in (1) computational biophysics and biochemistry, including biomolecular modeling, molecular dynamics  simulation and free energy calculation; (2) molecular docking and recognition for structure based drug design; (3) chemical physics of self-assembly in macromolecules. Broad knowledge in scientific computing and numerical algorithms. Strong written and oral communication skills. Proven ability of interdisciplinary research and collaboration.