NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near‐Physiological Conditions1. Issue 45 (20th September 2013)

• Record Type: Journal Article
• Authors: Gil, Sergio; Hošek, Tomáš; Solyom, Zsofia; Kümmerle, Rainer; Brutscher, Bernhard; Pierattelli, Roberta; Felli, Isabella C.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 45(2013)
• Page Start: 11808
• Page End: 11812
• Publication Date: 2013-09-20
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201304272
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>When approaching physiological conditions</bold>, solvent exchange of amide protons in intrinsically disordered proteins (IDPs) is so pronounced that it becomes a key feature to be considered in NMR experiment design. ¹³C NMR experiments recover information that is not accessible through amide proton detection, and solvent exchange can be used to increase sensitivity.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg4t72q59z" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>