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Automated structure determination from NMR spectra

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Abstract

Automated methods for protein structure determination by NMR have increasingly gained acceptance and are now widely used for the automated assignment of distance restraints and the calculation of three-dimensional structures. This review gives an overview of the techniques for automated protein structure analysis by NMR, including both NOE-based approaches and methods relying on other experimental data such as residual dipolar couplings and chemical shifts, and presents the FLYA algorithm for the fully automated NMR structure determination of proteins that is suitable to substitute all manual spectra analysis and thus overcomes a major efficiency limitation of the NMR method for protein structure determination.

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Acknowledgments

The author is financially supported by the Volkswagen Foundation and by a Grant-in-Aid for Scientific Research of the Japan Society for the Promotion of Science (JSPS).

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  1. Institute of Biophysical Chemistry, Goethe-University Frankfurt am Main, Max-von-Laue-Str. 9, 60438, Frankfurt am Main, Germany

    Peter Güntert

  2. Frankfurt Institute for Advanced Studies, Ruth-Moufang-Str. 1, 60438, Frankfurt am Main, Germany

    Peter Güntert

  3. Graduate School of Science, Tokyo Metropolitan University, 1-1 Minami-Osawa, Hachioji, Tokyo, 192-0397, Japan

    Peter Güntert

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Güntert, P. Automated structure determination from NMR spectra. Eur Biophys J 38, 129–143 (2009). https://doi.org/10.1007/s00249-008-0367-z

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