A COMPUTATIONAL-PROCEDURE FOR DETERMINING ENERGETICALLY FAVORABLE BINDING-SITES ON BIOLOGICALLY IMPORTANT MACROMOLECULES
A COMPUTATIONAL-PROCEDURE FOR DETERMINING ENERGETICALLY FAVORABLE BINDING-SITES ON BIOLOGICALLY IMPORTANT MACROMOLECULES
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DOI：
10.1021/jm00145a002
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发表时间：
1985-01-01
影响因子：
7.3
通讯作者：
GOODFORD, PJ
中科院分区：
文献类型：
--
作者：
GOODFORD, PJ
探针基团与已知结构的蛋白质的相互作用是在整个大分子及其周围的样品位置计算的，给出了一组能量值。探针包括水、甲基、胺氮、羧基氧和羟基。为每个探针计算适当能级的轮廓表面，并通过计算机图形与蛋白质结构一起显示。负能级的轮廓描绘了探针和蛋白质之间的吸引区域，特别是在已知的配体结合缝隙处。这些轮廓还可以识别其他吸引区域，并促进对蛋白质配体能量学的解释。它们可能对药物设计有价值。
The interaction of a probe group with a protein of known structure is computed at sample positions throughout and around the macromolecule, giving an array of energy values. The probes include water, the methyl group, amine nitrogen, carboxy oxygen and hydroxyl. Contour surfaces at appropriate energy levels are calculated for each probe and displayed by computer graphics together with the protein structure. Contours at negative energy levels delineate regions of attraction between probe and protein, and are found at known ligand binding clefts in particular. The contours also enable other regions of attraction to be identified and facilitate the interpretation of protein-ligand energetics. They may be of value for drug design.