Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins1. Issue 2 (28th November 2012)

• Record Type: Journal Article
• Authors: Huang, Jie‐rong; Ozenne, Valéry; Jensen, Malene Ringkjøbing; Blackledge, Martin
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 2(2013)
• Page Start: 687
• Page End: 690
• Publication Date: 2012-11-28
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201206585
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Conformational analysis</bold>: An approach to the prediction of RDCs from disordered protein chains, integrating the effect of nearest neighbors and the alignment characteristics of the statistical coil, is reported. NMR residual dipolar couplings (RDC) are sensitive probes of conformational sampling in unfolded proteins (see picture).<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1p994pzd" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>