Frontispiece: Probing Transient Conformational States of Proteins by Solid‐State R1ρ Relaxation‐Dispersion NMR Spectroscopy. Issue 17 (22nd April 2014)

• Record Type: Journal Article
• Authors: Ma, Peixiang; Haller, Jens D.; Zajakala, Jérémy; Macek, Pavel; Sivertsen, Astrid C.; Willbold, Dieter; Boisbouvier, Jérôme; Schanda, Paul
• Is Part Of: Angewandte Chemie international edition. Volume 53:Issue 17(2014)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2014-04-22
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201481771
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>In their Communication on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">page 4312 ff., </ext-link> P. Schanda et al. describe an NMR method used to probe conformational states of proteins. Information about the exchange kinetics, relative populations, and structures of the short‐lived state can be obtained.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg5cg0kx7q" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>