Wishart D S, Sykes B D
Department of Biochemistry, University of Alberta, Edmonton, Canada.
J Biomol NMR. 1994 Mar;4(2):171-80. doi: 10.1007/BF00175245.
A simple technique for identifying protein secondary structures through the analysis of backbone 13C 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 of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C 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 both 1H and 13C 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 from 1H and 13C chemical shifts, without recourse to NOE measurements.
本文描述了一种通过分析主链13C化学位移来识别蛋白质二级结构的简单技术。该技术基于化学位移指数[Wishart等人（1992年），《生物化学》，31卷，1647 - 1651页]，该指数最初是为分析1H(α)化学位移而开发的。通过扩展化学位移指数以纳入13C(α)、13C(β)和羰基13C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13C化学位移指数以产生二级结构的“共识”估计，可以实现超过92%的预测准确率。这表明肽和蛋白质的二级结构可以从1H和13C化学位移中准确获得，而无需借助NOE测量。
