Structural bioinformatics analysis of free cysteines in protein environments

CCUR > College of Natural Science and Engineering > College of Engineering > Department of Chemical & Materials Engineering > journal articles > Item 987654321/20908

Please use this identifier to cite or link to this item: https://irlib.pccu.edu.tw/handle/987654321/20908

Title:	Structural bioinformatics analysis of free cysteines in protein environments
Authors:	Ho, SL (Ho, Sheau Ling) Wang, AHJ (Wang, Andrew H. -J.)
Contributors:	化工系
Keywords:	SECONDARY STRUCTURE PATTERN-RECOGNITION RANGE INTERACTIONS SEQUENCE PREDICTION ALIGNMENT RESIDUES MATRIX
Date:	2009-03
Issue Date:	2011-12-09 10:59:48 (UTC+8)
Abstract:	Cysteine has been considered as a "hydrophilic" amino acid because of its pK(a) and its ability to form (weak)hydrogen bonds. However, cysteines are found mostly in hydrophobic environments, either in S-S (disulphide) form or in free cysteine form. When free cysteines are found on the surface of proteins, they are often involved in catalytic residues, as in cysteine proteases, P-loop phosphatases, etc. Additionally, a unique property of cysteines is that their side-chain volume is different from all other amino acids. This study is focused on the discrimination between structural versus active free cysteines based on a local environment analysis which does not appear to have been attempted previously. We have demonstrated the corresponding structural positions associated with free cysteines in their three-dimensional localization environment We examined protein samples including nine, sequenced, coronavirus proteases and cysteine-rich non-membrane proteins. Our present study shows that the sequential environments of free cysteines of coronavirus proteases are rather hydrophobic and that the free cysteines of non-membrane proteases have a higher amount of contacts to hydrophobic residues and lower amount of contacts to polar or charged residues. (C) 2008 Taiwan Institute of Chemical Engineers. Published by Elsevier B.V. All rights reserved.
Appears in Collections:	[Department of Chemical & Materials Engineering] journal articles

Files in This Item:

There are no files associated with this item.

Loading...