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The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data

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Summary

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 1Hα chemical shifts. By extending the Chemical-Shift Index to include 13Cα, 13Cβ 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.

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Authors and Affiliations

  1. Protein Engineering Network of Centres of Excellence, Department of Biochemistry, University of Alberta, T6G 2S2, Edmonton, AB, Canada

    David S. Wishart & Brian D. Sykes

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  1. David S. Wishart
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  2. Brian D. Sykes
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Additional information

Supplementary material is available in the form of a 10-page table (Table S1) describing the exact location of secondary structures in all 20 proteins as determined using the methods described in this paper. Requests for Table S1 should be directed to the authors.

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Wishart, D.S., Sykes, B.D. The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4, 171–180 (1994). https://doi.org/10.1007/BF00175245

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  • DOI: https://doi.org/10.1007/BF00175245

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