RELATIONSHIP BETWEEN NUCLEAR-MAGNETIC-RESONANCE CHEMICAL-SHIFT AND PROTEIN SECONDARY STRUCTURE
RELATIONSHIP BETWEEN NUCLEAR-MAGNETIC-RESONANCE CHEMICAL-SHIFT AND PROTEIN SECONDARY STRUCTURE
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DOI：
10.1016/0022-2836(91)90214-q
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发表时间：
1991-11-20
影响因子：
5.6
通讯作者：
RICHARDS, FM
中科院分区：
文献类型：
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作者：
WISHART, DS;SYKES, BD;RICHARDS, FM
对70多种蛋白质的1H核磁共振化学位移分配和二级结构命名的分析揭示了一些非常强的和意想不到的关系。在较小的数据库上进行的类似研究，13 C和15 N化学位移显示出与蛋白质二级结构同样强的相关性。这项工作中出现的更有趣的结果是发现，当以螺旋构型放置时，所有20种天然存在的氨基酸的平均αa-1H高场位移为百万分之0.39（来自无规卷曲值）。以类似的方式，当残基被置于β链或延伸构型时，发现α-1H化学位移平均向低场移动百万分之0.37。酰胺1H、羰基13 C、α-13 C和酰胺15 N的化学位移也有类似的变化。化学位移和蛋白质构象之间的其他关系也被发现;特别是螺旋偶极效应和酰胺质子化学位移之间的相关性，以及α-质子化学位移和主链柔性之间的关系。此外，α-质子化学位移和主链二面角之间的有用的关系，以及酰胺质子化学位移和氢键效应之间的相关性被证明。
An analysis of the1H nuclear magnetic resonance chemical shift assignments and secondary structure designations for over 70 proteins has revealed some very strong and unexpected relationships. Similar studies, performed on smaller databases, for13C and15N chemical shifts reveal equally strong correlations to protein secondary structure. Among the more interesting results to emerge from this work is the finding that all 20 naturally occurring amino acids experience a mean αa-1H upfield shift of 0.39 parts per million (from the random coil value) when placed in a helical configuration. In a like manner, the α-1H chemical shift is found to move downfield by an average of 0.37 parts per million when the residue is placed in a β-strand or extended configuration. Similar changes are also found for amide1H, carbonyl13C, α-13C and amide15N chemical shifts. Other relationships between chemical shift and protein conformation are also uncovered; in particular, a correlation between helix dipole effects and amide proton chemical shifts as well as a relationship between α-proton chemical shifts and main-chain flexibility. Additionally, useful relationships between α-proton chemical shifts and backbone dihedral angles as well as correlations between amide proton chemical shifts and hydrogen bond effects are demonstrated.