RECOGNITION OF DISTANTLY RELATED PROTEINS THROUGH ENERGY CALCULATIONS
RECOGNITION OF DISTANTLY RELATED PROTEINS THROUGH ENERGY CALCULATIONS
复制标题
DOI：
10.1002/prot.340190206
复制
发表时间：
1994-06-01
期刊：
影响因子：
--
通讯作者：
ARGOS, P
中科院分区：
文献类型：
--
作者：
ABAGYAN, R;FRISHMAN, D;ARGOS, P
一种新的方法来检测蛋白质序列和已知的三维结构之间的远程关系基于直接能量计算和不依赖于统计已经发展。残基占据结构模板上给定位置的可能性由取代侧链构象明确预测后的稳定自由能估计来表示。基于这些能量值并通过增加残基自交换值进行修饰的图谱矩阵成功地预测了热休克蛋白和球蛋白序列分别与肌动蛋白和藻蓝蛋白三维结构的相容性。该方法的高灵敏度使其成为预测快速增长的蛋白质序列的三维折叠的独特工具。(C) 1994 Wiley-Liss, Inc。
A new method to detect remote relationships between protein sequences and known three-dimensional structures based on direct energy calculations and without reliance on statistics has been developed. The likelihood of a residue to occupy a given position on the structural template was represented by an estimate of the stabilization free energy made after explicit prediction of the substituted side chain conformation. The profile matrix derived from these energy values and modified by increasing the residue self-exchange values successfully predicted compatibility of heat-shock protein and globin sequences with the three-dimensional structures of actin and phycocyanin, respectively, from a full protein sequence databank search. The high sensitivity of the method makes it a unique tool for predicting the three-dimensional fold for the rapidly growing number of protein sequences. (C) 1994 Wiley-Liss, Inc.