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Advances in automated NMR protein structure determination

Published online by Cambridge University Press:  17 March 2011

Paul Guerry  and
Torsten Herrmann
Paul Guerry
Affiliation:
Centre Européen de RMN à très Hauts Champs, Université de Lyon/CNRS/ENS, Lyon/UCB Lyon 1, 5 rue de la Doua, 69100 Villeurbanne, France
Torsten Herrmann*
Affiliation:
Centre Européen de RMN à très Hauts Champs, Université de Lyon/CNRS/ENS, Lyon/UCB Lyon 1, 5 rue de la Doua, 69100 Villeurbanne, France
*
*Author for correspondence: Torsten Herrmann, Centre Européen de RMN à très Hauts Champs, Université de Lyon/CNRS/ENS, Lyon/UCB Lyon 1, 5 rue de la Doua, 69100 Villeurbanne, France. Tel.: +33 (0)423 233882; Email: torsten.herrmann@ens-lyon.fr
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Abstract

Around half of all protein structures solved nowadays using solution-state nuclear magnetic resonance (NMR) spectroscopy have been because of automated data analysis. The pervasiveness of computational approaches in general hides, however, a more nuanced view in which the full variety and richness of the field appears. This review is structured around a comparison of methods associated with three NMR observables: classical nuclear Overhauser effect (NOE) constraint gathering in contrast with more recent chemical shift and residual dipole coupling (RDC) based protocols. In each case, the emphasis is placed on the latest research, covering mainly the past 5 years. By describing both general concepts and representative programs, the objective is to map out a field in which – through the very profusion of approaches – it is all too easy to lose one's bearings.

Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 44 , Issue 3 , August 2011 , pp. 257 - 309
Copyright
Copyright © Cambridge University Press 2011

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