SECONDARY AND TERTIARY STRUCTURAL EFFECTS ON PROTEIN NMR CHEMICAL-SHIFTS - AN ABINITIO APPROACH
SECONDARY AND TERTIARY STRUCTURAL EFFECTS ON PROTEIN NMR CHEMICAL-SHIFTS - AN ABINITIO APPROACH
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DOI：
10.1126/science.8502992
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发表时间：
1993-06-04
期刊：
影响因子：
56.9
通讯作者：
OLDFIELD, E
中科院分区：
文献类型：
--
作者：
DEDIOS, AC;PEARSON, JG;OLDFIELD, E
最近的理论发展使预测蛋白质中的H-1、C-13、N-15和F-19核磁共振化学位移成为可能，并为分析二级和三级结构以及探测蛋白质静电学提供了新的方法。对于C-13、Phi、psi扭角对Calpha和Cbeta的屏蔽起主导作用，但氢键和静电的加入更符合实验结果。对于N-15H，侧链(Chi1)扭转角也很重要，最近邻序列效应也是重要的，而对于H-1N，氢键特别重要。对于F-19，微弱或远程静电场主导了F-19的屏蔽不等价性。预测已知或测试结构中蛋白质的化学位移的能力为结构优化或确定开辟了新的途径，特别是对于浓缩系统。
Recent theoretical developments permit the prediction of H-1, C-13, N-15, and F-19 nuclear magnetic resonance chemical shifts in proteins and offer new ways of analyzing secondary and tertiary structure as well as for probing protein electrostatics. For C-13, phi,psi torsion angles dominate shielding for Calpha and Cbeta, but the addition of hydrogen bonding and electrostatics gives even better accord with experiment. For N-15H, side chain (chi1) torsion angles are also important, as are nearest neighbor sequence effects, whereas for H-1N, hydrogen bonding is particularly significant. For F-19, weak or long-range electrostatic fields dominate F-19 shielding nonequivalencies. The ability to predict chemical shifts in proteins from known or test structures opens new avenues to structure refinement or determination, especially for condensed systems.