摘要
Protein folding, one of the most fundamental events in cells, is very complex and difficult to be characterized in detail. Although much progress, especially the energy landscape theory, has been made based on studies on some small and single domain proteins, this important problem in molecular biology has not been completely solved. Based on the simplified protein models, such as the single bead-model for residues and the simplified Go-like proteins between the residues, we have made some studies on: folding of protein Tendamistat, folding of an unfrustrated substrate protein encapsulated in a chaperonin-like cavity, folding of protein BBL downhill behavior, and dimerization of two proteins in a confined space, and so on. We have also made intensive simulations based on all-atom proteins model to study: folding process of trpzip2-hairpin and folding of Cys2His2-type zinc-finger motif. These studies provide significant insight into the general mechanisms of protein folding.
参考文献：
[1] Wei Wang, Wei-Xin Xu, Yaakov Levy, E. Trizac, and P. G. Wolynes, Molecular Crowding Effects on the Kinetics and Thermodynamics of Protein Dimerization，PNAS, 106, 5517 (2009).
[2] W. F. Li, J. Zhang, J. Wang, and W. Wang, Metal-coupled folding of C2H2 zinc-finger, JACS, 130, 892 (2008).
[3] X. P. Zhang, F. Liu, Z. Cheng, and W. Wang, Cell fate decision mediated by p53 pulses, PNAS, 106, 12245 (2009).
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