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_ε-C_ζ 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