IMPROVED EFFICIENCY OF PROTEIN STRUCTURE CALCULATIONS FROM NMR DATA USING THE PROGRAM DIANA WITH REDUNDANT DIHEDRAL ANGLE CONSTRAINTS
IMPROVED EFFICIENCY OF PROTEIN STRUCTURE CALCULATIONS FROM NMR DATA USING THE PROGRAM DIANA WITH REDUNDANT DIHEDRAL ANGLE CONSTRAINTS
复制标题
DOI：
10.1007/bf02192866
复制
发表时间：
1991-01-01
影响因子：
2.7
通讯作者：
WUTHRICH K
中科院分区：
文献类型：
--
作者：
GUNTERT P;WUTHRICH K
描述了一种使用可变目标函数方法计算蛋白质 NMR 结构的新策略（Braun, W. 和 G.hivin.o, N. (1985) J. Mol. Biol., 186, 611），该策略利用从完整结构的初步计算得出的冗余二面角约束 (REDAC)。 REDAC 方法根据蛋白质结构的复杂性，将使用程序 DIANA 获得一组可接受的构象异构体的计算时间减少了 5-100 倍，并保留了构象空间的良好采样。
A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and G.hivin.o, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of redundant dihedral angle constraints (REDAC) derived from preliminary calculations of the complete structure. The REDAC approach reduces the computation time for obtaining a group of acceptable conformers with the program DIANA 5-100-fold, depending on the complexity of the protein structure, and retains good sampling of conformation space.