Magyar Csaba, Gromiha M Michael, Pujadas Gerard, Tusnády Gábor E, Simon István
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences H-1518 Budapest, PO Box 7, Hungary.
Nucleic Acids Res. 2005 Jul 1;33(Web Server issue):W303-5. doi: 10.1093/nar/gki409.
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.
预计在蛋白质稳定化过程中发挥关键作用的残基[稳定残基(SRs)],主要通过结合多种方法来选择,这些方法基于给定残基与其空间邻域(而非序列邻域)的相互作用,并考虑残基的进化保守性。如果一个残基具有高周围疏水性、高长程有序性、高保守得分且属于一个稳定中心,则将其选为稳定残基。详细讨论了所有这些参数的定义以及用于识别SRs的阈值。识别SRs的算法最初是为TIM桶状蛋白开发的[M. M. Gromiha, G. Pujadas, C. Magyar, S. Selvaraj, and I. Simon (2004), Proteins, 55, 316 - 329],现在已推广到所有已知三维结构的蛋白质。SRs可应用于蛋白质工程和同源建模,也有助于解释某些具有显著稳定性的折叠。SRide服务器位于http://sride.enzim.hu 。