NDLI: 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

Content Provider	Semantic Scholar
Author	Gerecht, Karola Figueiredo, Angelo M. Hansen, D. Flemming
Copyright Year	2017
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.
Starting Page	10062
Ending Page	10065
Page Count	4
File Format	PDF HTM / HTML
DOI	10.1039/c7cc04821a
PubMed reference number	28840203
Journal	Medline
Volume Number	53
Alternate Webpage(s)	http://discovery.ucl.ac.uk/1572357/1/c7cc04821a.pdf
Alternate Webpage(s)	http://www.rsc.org/suppdata/c7/cc/c7cc04821a/c7cc04821a1.pdf
Alternate Webpage(s)	https://doi.org/10.1039/c7cc04821a
Journal	Chemical communications
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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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