일시 : 2017년 9월 27일(수) 오후5시-7시
장소 : 과학관 604호
연사 : 유우경 교수님(DGIST,뇌인지과학전공)
Proteins play a critical role in cellular function. The study of proteins at the molecular level is of fundamental importance in not only the determination of biological mechanism but also the searching for the new biological function. A wide variety of biophysical experimental tools exist for studying proteins such as circular dichroism, small angle scattering, fluorescence energy transfer, and hydrogen exchange (HX). HX, when combined with NMR and mass spectroscopy, can monitor the breaking of individual H-bonds, is one of the best methods for studying the conformational change of protein with amino acid resolution. In addition, computational methods are integral to the studying protein function. This includes the application of theoretical modeling, coarse graining simulation, all atom molecular dynamics and quantum calculations. Even though simulation provides a wealth of information, simulation must be experimentally validated.
Here I present both experimental and computational studies of folding cooperativity, stability, dynamics and conformational change for a variety of proteins. I show how one can compare experimental HX data and computer simulations, with the goal of providing a general protocol for validating the ability of simulations to accurately capture rare structural fluctuations.