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出 处:《Bulletin of the Chinese Academy of Sciences》2014年第3期251-251,共1页中国科学院院刊(英文版)
基 金:supported by the National Natural Science Foundation of China(Grant No.20925313 and 21090342);the National Basic Research Program of China(Grant No.2006CB910302);the Chinese Academy of Sciences Innovation Program(Grant No.KJCX2-YW-W25)
摘 要:Protein could carry out its biological function only when it is folded into the right conformation,and the conformation might be changing during the activation process,therefore protein dynamical structure provides a key clue to understand its function.Although many protein static structures have been resolved by X-ray crystallography,2D NM and cryoelectron microscope at atomic level,the static structure could be different from the dynamical structure,especially under physiological condition.In their continuous effort to study the protein dynamical structure with temperature-jump time-resolved infrared spectroscopy(Biophys.J.2007,93,2756–2766;Biophys.J.2009,97,2756–2766),a team lead by Prof.WENG Yuxiang from the Institute of Physics(IOP),Chinese Academy of Sciences recently collaborated with Prof.CHANGProtein could carry out its biological function only when it is folded into the right conformation, and the conformation might he changing during the activation process, therefore protein dynamical structure provides a key clue to understand its function. Although many protein static structures have been resolved by X-ray crystallography, 2D NM and cryoelectron microscope at atomic level, the static structure could be different from the dynamical structure, especially under physiological condition.
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