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Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.


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 N?-C? 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.

SUBMITTER: Gerecht K 

PROVIDER: S-EPMC5708338 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.

Gerecht Karola K   Figueiredo Angelo Miguel AM   Hansen D Flemming DF  

Chemical communications (Cambridge, England) 20170825 72


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 N<sub>ε</sub>-C<sub>ζ</sub> 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. ...[more]

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