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