Ligand-induced protein responses and mechanical signal propagation described by linear response theories
Yang, L.-W.*; 北尾 彰朗*; Huang, B.-C.*; 郷 信広*
Yang, L.-W.*; Kitao, Akio*; Huang, B.-C.*; Go, Nobuhiro*
In this study, a general linear response theory (LRT) is formulated to describe time-dependent and -independent protein conformational changes upon CO binding with myoglobin. Using the theory, we are able to monitor protein relaxation in two stages. The slower relaxation is found to occur from 4.4 to 81.2 picoseconds and the time constants characterized for a couple of aromatic residues agree with those observed by UV Resonance Raman (UVRR) spectrometry and time resolved X-ray crystallography. The faster "early responses", triggered as early as 400 femtoseconds, can be best described by the theory when impulse forces are used. The newly formulated theory describes the mechanical propagation following ligand-binding as a function of time, space and types of the perturbation forces. The "disseminators", defined as the residues that propagate signals throughout the molecule the fastest among all the residues in protein when perturbed, are found evolutionarily conserved and the mutations of which have been shown to largely change the CO rebinding kinetics in myoglobin.
使用言語 : English
掲載資料名 : Biophysical Journal
: 107
: 6
ページ数 : p.1415 - 1425
発行年月 : 2014/09
出版社名 : Biophysical Society
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登録番号 : AA20140460
抄録集掲載番号 : 42001398
論文投稿番号 : 15024
Accesses  (From Jun. 2, 2014)
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