Protein Conformational Space Populated in Solution Probed with Aromatic Residual Dipolar 13C–1H Couplings. Issue 6 (12th March 2013)

• Record Type: Journal Article
• Authors: Sathyamoorthy, Bharathwaj; Singarapu, Kiran K.; Garcia, Angel E.; Szyperski, Thomas
• Is Part Of: Chembiochem. Volume 14:Issue 6(2013)
• Page Start: 684
• Page End: 688
• Publication Date: 2013-03-12
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201300016
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The use of aromatic</bold> ^{<bold>13</bold>} <bold>C–¹H residual dipolar couplings</bold> (RDCs) to probe the conformational space populated in solution is demonstrated for the protein BPTI. RDCs allow one to assess accuracy of atomic resolution structures and potentially to characterize low‐populated subspaces corresponding to "excited states" in conformationally labile systems. They also allow one to assess sampling accuracy of molecular dynamics simulations.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1x4z0pdr" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>