Speaker：Shasha Feng （冯莎莎） Meichen Fang （方美琛） Zhecheng Huang （黄哲成） Da Teng (滕达)

Abstract:

Protein folding status influences the function of protein, and has been playing a major role in disease and drug design. However, it is not easy to investigate whether the membrane protein of GPCR family is folding well in the lipid bilayer, or whether a key player in certain cell signaling pathway is folded to correct conformation.  The first few tools come out in mind would be structure biology tools like NMR, cryo-EM, X-Ray mostly. However they sample only the stable conformation in artificial context, for example, the membrane protein are first purified in detergent so the conformation might be different from the one in real biological membrane. Molecular dynamics simulation has been a trend recently to simulate the protein in more biological environment. What’s more, its capacity to calculate the energy landscape facilitates understanding protein folding and binding. As a prospective powerful tool, MD simulation is worth biologists’ attention.

Guest information:

Dr. Chen Song (PKU)

http://cqb.pku.edu.cn/songgroup/

Recommend Literatures：

Review:

Gelpi, J., Hospital, A., Goñi, R., & Orozco, M. (2015). Molecular dynamics simulations: advances and applications. Advances And Applications In Bioinformatics And Chemistry, 37. http://dx.doi.org/10.2147/aabc.s70333

Papers:

1 Higo, J., Nishimura, Y., & Nakamura, H. (2011). A Free-Energy Landscape for Coupled Folding and Binding of an Intrinsically Disordered Protein in Explicit Solvent from Detailed All-Atom Computations. Journal Of The American Chemical Society, 133(27), 10448-10458. http://dx.doi.org/10.1021/ja110338e

2 Prigozhin, M., Chao, S., Sukenik, S., Pogorelov, T., & Gruebele, M. (2015). Mapping fast protein folding with multiple-site fluorescent probes. Proceedings Of The National Academy Of Sciences, 112(26), 7966-7971.

http://dx.doi.org/10.1073/pnas.1422683112