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 which was originally developed for the analysis of 1Ha chemical shifts. By extending the Chemical-Shift Index to include 13Ca, 13Cb, and carbonyl 13C chemical shifts, it is now possible to user 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 predicitive accuract in excesss of 92%. This suggests that the secondary structure of peptides and proteinscan be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements.
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