Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR. Issue 72 (25th August 2017)

• Record Type: Journal Article
• Authors: Gerecht, Karola; Figueiredo, Angelo Miguel; Hansen, D. Flemming
• Is Part Of: Chemical communications. Volume 53:Issue 72(2017)
• Page Start: 10062
• Page End: 10065
• Publication Date: 2017-08-25
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c7cc04821a
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : A new NMR-based method is presented to determine the rotational dynamics around the Nε –Cζ bond of arginine to characterise the interactions mediated by arginine side chains. Abstract : Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the Nε –Cζ bond of arginine side chains. An application to a 19 kDa protein shows that the strengths of interactions involving arginine side chains can be characterised.