SRide:: a server for identifying stabilizing residues in proteins

被引:101
|
作者
Magyar, C
Gromiha, MM
Pujadas, G
Tusnády, GE
Simon, I
机构
[1] Hungarian Acad Sci, Biol Res Ctr, Inst Enzymol, H-1518 Budapest, Hungary
[2] Natl Inst Adv Ind Sci & Technol, Computat Biol Res Ctr, Koto Ku, Tokyo 1350064, Japan
[3] Univ Rovira & Virgili, Dept Bioquim & Biotechnol, Res Grp Wine & Hlth, Tarragona 43007, Catalonia, Spain
关键词
D O I
10.1093/nar/gki409
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Residues expected to play key roles in the stabilization of proteins [stabilizing residues (SRs)] are selected by combining several methods based mainly on the interactions of a given residue with its spatial, rather than its sequential neighborhood and by considering the evolutionary conservation of the residues. A residue is selected as a stabilizing residue if it has high surrounding hydrophobicity, high long-range order, high conservation score and if it belongs to a stabilization center. The definition of all these parameters and the thresholds used to identify the SRs are discussed in detail. The algorithm for identifying SRs was originally developed for TIM-barrel proteins [M. M. Gromiha, G. Pujadas, C. Magyar, S. Selvaraj, and I. Simon (2004), Proteins, 55, 316-329] and is now generalized for all proteins of known 3D structure. SRs could be applied in protein engineering and homology modeling and could also help to explain certain folds with significant stability. The SRide server is located at http://sride.enzim.hu.
引用
收藏
页码:W303 / W305
页数:3
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