DICP OpenIR
学科主题物理化学
Investigating the molecular mechanisms of protein folding kinetics using a tightly joined experimental and theoretical approach
Zhuang W(庄巍)
会议名称China-Israel Workshop on: Dynamics and Control of Quntum Systems
会议日期2010-3-23
2010-03-23
会议地点以色列
其他题名通过实验与理论密切结合来研究蛋白质折叠动力学机理
页码2/1
部门归属十一室
主办者以色列科学基金会
英文摘要The response of complex molecules to sequences of femtosecond infrared pulses provides a unique window into their structure, dynamics, and fluctuating environments. In this talk, I will survey the basic principles of modern two-dimensional infrared (2DIR) spectroscopy, which analogous to those of multidimensional NMR spectroscopy. The perturbative approach for computing the nonlinear optical response of coupled localized chromophores is introduced and applied to the amide backbone transitions of proteins, liquid water, membrane lipids, and amyloid fibrils. The signals are analyzed using classical molecular dynamics simulations combined with an effective fluctuating Hamiltonian for coupled localized anharmonic vibrations whose dependence on the local electrostatic environment is parameterized by an ab initio map. Chirality induced techniques which dramatically enhance the resolution are demonstrated. Signatures of conformational and hydrogen bonding fluctuations, protein folding, and chemical-exchange processes are discussed.
语种中文
文献类型会议论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/114044
专题中国科学院大连化学物理研究所
通讯作者Zhuang W(庄巍)
推荐引用方式
GB/T 7714
Zhuang W. Investigating the molecular mechanisms of protein folding kinetics using a tightly joined experimental and theoretical approach[C],2010:2/1.
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