CRASP：一个用于分析蛋白质序列多序列比对中协同替换的程序。
CRASP: a program for analysis of coordinated substitutions in multiple alignments of protein sequences.
作者信息
Afonnikov Dmitry A, Kolchanov Nikolay A
机构信息
Institute of Cytology and Genetics, SB RAS, Novosibirsk, Russia.
出版信息
Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W64-8. doi: 10.1093/nar/gkh451.
Abstract
Recent results suggest that during evolution certain substitutions at protein sites may occur in a coordinated manner due to interactions between amino acid residues. Information on these coordinated substitutions may be useful for analysis of protein structure and function. CRASP is an Internet-available software tool for the detection and analysis of coordinated substitutions in multiple alignments of protein sequences. The approach is based on estimation of the correlation coefficient between the values of a physicochemical parameter at a pair of positions of sequence alignment. The program enables the user to detect and analyze pairwise relationships between amino acid substitutions at protein sequence positions, estimate the contribution of the coordinated substitutions to the evolutionary invariance or variability in integral protein physicochemical characteristics such as the net charge of protein residues and hydrophobic core volume. The CRASP program is available at http://wwwmgs.bionet.nsc.ru/mgs/programs/crasp/.
摘要
最近的研究结果表明，在进化过程中，由于氨基酸残基之间的相互作用，蛋白质位点的某些替换可能会以协同的方式发生。这些协同替换的信息可能有助于分析蛋白质的结构和功能。CRASP是一种可通过互联网获取的软件工具，用于检测和分析蛋白质序列多序列比对中的协同替换。该方法基于对序列比对中一对位置上物理化学参数值之间相关系数的估计。该程序使用户能够检测和分析蛋白质序列位置上氨基酸替换之间的成对关系，估计协同替换对蛋白质整体物理化学特征（如蛋白质残基的净电荷和疏水核心体积）的进化不变性或变异性的贡献。CRASP程序可在http://wwwmgs.bionet.nsc.ru/mgs/programs/crasp/获取。
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