GEOMETRY OF INTERPLANAR RESIDUE CONTACTS IN PROTEIN STRUCTURES
GEOMETRY OF INTERPLANAR RESIDUE CONTACTS IN PROTEIN STRUCTURES
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DOI：
10.1073/pnas.91.20.9297
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发表时间：
1994-09-27
影响因子：
11.1
通讯作者：
KARLIN, S
中科院分区：
文献类型：
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作者：
BROCCHIERI, L;KARLIN, S
相互作用的侧链平面基团（芳香族，胍，酰胺，羧基，咪唑）的相对空间配置进行了分析，为186个非同源的解析良好的蛋白质结构。酰胺或羧基平面基团与其它平面基团的二面角符合平面的随机分布。相比之下，紧密的芳香环或组氨酸环与芳香残基相互作用的平面之间的二面角是显着的非随机的，显示出近似均匀的分布。我们的研究结果表明，边缘到边缘和边缘到中心的残留物平面部分的空间配置是普遍的，而完整的堆叠配置是罕见的。静电力是侧链平面基团之间的相互作用的几何形状的一个主要决定因素的假设进行了讨论。
The relative spatial disposition of interacting side-chain planar groups (aromatic, guanidinium, amide, carboxyl, imidazole) is analyzed for 186 non-homologous well-resolved protein structures. The dihedral angle of amide or carboxyl planar groups with other planar groups accords with a random distribution of planes. By contrast, the dihedral angle of the planes between close aromatic rings or of the histidine ring interacting with aromatic residues is significantly nonrandom, showing an approximately uniform distribution. Our results indicate that edge-to edge and edge-to-center spatial dispositions of residue planar sections are prevalent, while complete stacking configurations are uncommon. The hypothesis that electrostatic forces are a major determinant of the geometry of interactions between side-chain planar groups is discussed.