Intrinsic coordination for revealing local structural changes in protein folding-unfolding

doi:10.1039/c5cp06309d

淡江大學機構典藏 > 理學院 > 化學學系暨研究所 > 期刊論文 > Item 987654321/117143

jsp.display-item.identifier=請使用永久網址來引用或連結此文件: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/117143

题名:	Intrinsic coordination for revealing local structural changes in protein folding-unfolding
作者:	Shiu, Ying-Jen;Hayashi, Michitoshi;Shih, Orion;Su, Charlene;Tsai, Min-Yeh;Yeh, Yi-Qi;Su, Chun-Jen;Huang, Yu-Shan;Lin, Sheng-Hsien;Jeng, U-Ser
日期:	2015-12-23
上传时间:	2019-09-26 12:11:03 (UTC+8)
出版者:	Royal Society of Chemistry
摘要:	With a deformed object of a rigid rod inside, the local dislocations may be tracked relatively easily with respect to the internal rigid rod. We apply this concept on protein folding-unfolding to track the internal structural changes of an unfolded protein in solution. Proposed here is a protein internal coordination based on the major axis X of an ellipsoidal protein and the stable intrinsic transition dipole moment μ of the protein during unfolding. In this methodology, small-angle X-ray scattering (SAXS) is used to provide the protein global morphologies in the native and unfolded states. Furthermore, time-resolved fluorescence anisotropy (TRFA) provides the relative orientation between X and μ of Trp59 of the model protein cytochrome c. Hence observed in the protein unfolding with denaturants, acid, urea, or GuHCl, is the elongation of the native protein conformation along a reoriented protein major axis; accompanied are the different extents of relocations of the terminal α helices and loop structures of the protein in the corresponding unfolding.
關聯:	Physical Chemistry Chemical Physics, 18(4), 3179
DOI:	10.1039/c5cp06309d
显示于类别:	[化學學系暨研究所] 期刊論文

文件中的档案:

档案	描述	大小	格式	浏览次数
index.html		0Kb	HTML	118	检视/开启
Intrinsic coordination for revealing local structural changes in protein folding-unfolding.pdf		2287Kb	Adobe PDF	1	检视/开启

在機構典藏中所有的数据项都受到原著作权保护.

TAIR相关文章

数据加载中.....