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1. Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7cc04821a

Author

Gerecht, Karola, Figueiredo, Angelo Miguel, and Hansen, D. Flemming

Subjects
Chemistry, Nitrogen Isotopes, Protein Conformation, Muramidase, Carbon-13 Magnetic Resonance Spectroscopy, Arginine, Guanidines
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., 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.

Published
2017

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