A Computational Study of the Effects of 13C–13C Scalar Couplings on 13C CEST NMR Spectra: Towards Studies on a Uniformly 13C‐Labeled Protein. Issue 14 (19th June 2013)

• Record Type: Journal Article
• Authors: Vallurupalli, Pramodh; Bouvignies, Guillaume; Kay, Lewis E.
• Is Part Of: Chembiochem. Volume 14:Issue 14(2013)
• Page Start: 1709
• Page End: 1713
• Publication Date: 2013-06-19
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201300230
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Read the label:</bold> The NMR CEST experiment can be used to reconstruct spectra of sparsely populated, transiently formed protein conformers so long as they exchange with a highly populated ground state with rates of 20–300 s⁻¹. Here we establish that accurate ¹³C chemical shifts of side‐chain carbon nuclei can be obtained from uniformly ¹³C‐labeled samples, without interference from the coupled ¹³C spin network.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg3hdpvh4p" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>