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HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains

2006; Wiley; Volume: 44; Issue: S1 Linguagem: Inglês

10.1002/mrc.1825

1097-458X

Paul Schanda, Vincent Forge, Bernhard Brutscher,

RNA and protein synthesis mechanisms

Magnetic Resonance in ChemistryVolume 44, Issue S1 p. S177-S184 Methodology HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains Paul Schanda, Paul Schanda Institut de Biologie Structurale, Jean-Pierre Ebel C.N.R.S.-C.E.A.-UJF, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, FranceSearch for more papers by this authorVincent Forge, Vincent Forge Biophysique Moléculaire et Cellulaire, Unité Mixte de Recherche 5090, Département Réponse et Dynamique Cellulaires, CEA-Grenoble, 38054 Grenoble Cedex 9, FranceSearch for more papers by this authorBernhard Brutscher, Corresponding Author Bernhard Brutscher [email protected] Institut de Biologie Structurale, Jean-Pierre Ebel C.N.R.S.-C.E.A.-UJF, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, FranceLaboratoire de RMN, Institut de Biologie Structurale, Jean-Pierre Ebel, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, France.===Search for more papers by this author Paul Schanda, Paul Schanda Institut de Biologie Structurale, Jean-Pierre Ebel C.N.R.S.-C.E.A.-UJF, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, FranceSearch for more papers by this authorVincent Forge, Vincent Forge Biophysique Moléculaire et Cellulaire, Unité Mixte de Recherche 5090, Département Réponse et Dynamique Cellulaires, CEA-Grenoble, 38054 Grenoble Cedex 9, FranceSearch for more papers by this authorBernhard Brutscher, Corresponding Author Bernhard Brutscher [email protected] Institut de Biologie Structurale, Jean-Pierre Ebel C.N.R.S.-C.E.A.-UJF, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, FranceLaboratoire de RMN, Institut de Biologie Structurale, Jean-Pierre Ebel, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, France.===Search for more papers by this author First published: 06 July 2006 https://doi.org/10.1002/mrc.1825Citations: 56AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract Structure elucidation of proteins by either NMR or X-ray crystallography often requires the screening of a large number of samples for promising protein constructs and optimum solution conditions. For large-scale screening of protein samples in solution, robust methods are needed that allow a rapid assessment of the folding of a polypeptide under diverse sample conditions. Here we present HET-SOFAST NMR, a highly sensitive new method for semi-quantitative characterization of the structural compactness and heterogeneity of polypeptide chains in solution. On the basis of one-dimensional 1H HET-SOFAST NMR data, obtained on well-folded, molten globular, partially- and completely unfolded proteins, we define empirical thresholds that can be used as quantitative benchmarks for protein compactness. For 15N-enriched protein samples, two-dimensional 1H-15N HET-SOFAST correlation spectra provide site-specific information about the structural heterogeneity along the polypeptide chain. Copyright © 2006 John Wiley & Sons, Ltd. Citing Literature Volume44, IssueS1Special Issue: NMR of Proteins in SolutionJuly 2006Pages S177-S184 RelatedInformation