Viswanadhan V N, Sundaram K
Int J Pept Protein Res. 1983 Feb;21(2):190-5. doi: 10.1111/j.1399-3011.1983.tb03092.x.
Some well sequenced classes of homologous proteins have been analysed in the light of their representative tertiary structures to reveal the nature of structural conservation during protein evolution. Within 'the sphere of influence' around conserved residue sites preferential association of other conservative sites has been observed to be a feature of natural selection valid for all residue types. An information theory approach evolved to examine residue variability reveals that even some non-conservative sites scaffold clusters of high biochemical specificity and intermediate folding units.
一些测序良好的同源蛋白质类别已根据其代表性三级结构进行分析,以揭示蛋白质进化过程中结构保守的本质。在保守残基位点周围的“影响范围内”,已观察到其他保守位点的优先关联是对所有残基类型均有效的自然选择特征。一种用于检查残基变异性的信息论方法表明,即使是一些非保守位点也构成了高生化特异性簇和中间折叠单元。