Global and local structural changes of cytochrome c and lysozyme characterized by a multigroup unfolding process

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题名:	Global and local structural changes of cytochrome c and lysozyme characterized by a multigroup unfolding process
作者:	Shiu, Y.-J.a, Jeng, U.-S.bf , Huang, Y.-S.b, Lai, Y.-H.b, Lu, H.-F.c, Liang, C.-T.a, Hsu, I.-J.d, Su, C.-H.b, Su, C.a, Chao, I.c, Su, A.-C.e, Lin, S.-H.
关键词:	article;chemical model;chemical structure;chemistry;computer simulation;crystallography;methodology;protein conformation;protein denaturation;protein folding;ultrastructure
日期:	2008
上传时间:	2013-05-21T09:09:13Z (UTC)
出版者:	Department of Chemistry, Tunghai University
摘要:	Equilibrium unfolding behaviors of cytochrome c and lysozyme induced by the presence of urea (0-10 M) as well as changes in temperature (295-363 K) or pH (1.8-7) are examined via small-angle x-ray scattering and spectroscopic techniques, including circular dichroism and optical absorption. Denaturant and temperature effects are incorporated into the free energy expression for a general multigroup unfolding process. Results indicate that there are at least four unfolding groups in the temperature-, urea-, or pH-induced unfolding of cytochrome c: two of these are related to the prosthetic heme group, and the other two correspond, respectively, to the unfolding of α-helices and global changes in protein morphology that are largely unaccounted for by the first two groups. In contrast, the unfolding of lysozyme approximately follows a simple one-group process. A modified mean-field Ising model is adopted for a coherent description of the unfolding behaviors observed. Thermodynamic parameters extracted from simple denaturing processes, on the basis of the Ising model, can closely predict unfolding behaviors of the proteins in compounded denaturing environments. ? 2008 by the Biophysical Society.
關聯:	Biophysical Journal 94 (12) , pp. 4828-4836
显示于类别:	[化學系所] 期刊論文

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