The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
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DOI：
10.1007/bf00175245
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发表时间：
1994-03
影响因子：
2.7
通讯作者：
D. Wishart;B. Sykes
中科院分区：
文献类型：
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作者：
D. Wishart;B. Sykes
描述了一种通过骨架13 C化学位移分析鉴定蛋白质二级结构的简单技术。它是基于化学位移指数[Wishart et al.（1992）Biochemistry，31，1647-1651]，该指数最初是为分析1H α化学位移而开发的。通过将化学位移指数扩展到包括13 C α、13 C β和羰基13 C化学位移，现在可以使用四个独立的化学位移测量来识别和定位蛋白质二级结构。结果表明，通过结合1H和13 C化学位移指数，以产生一个“共识”的二级结构的估计，它是可能实现的预测精度超过92%。这表明肽和蛋白质的二级结构可以从1H和13 C化学位移中准确地获得，而不依赖于NOE测量。
A simple technique for identifying protein secondary structures through the analysis of backbone13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992)Biochemistry,31, 1647–1651] which was originally developed for the analysis of1Hαchemical shifts. By extending the Chemical-Shift Index to include13Cα,13Cβand carbonyl13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both1H and13C chemical-shift indices to produce a ‘consensus’ estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from1H and13C chemical shifts, without recourse to NOE measurements.