Conformational dependence of 13C shielding and coupling constants for methionine methyl groups.

ABSTRACT: Methionine residues fulfill a broad range of roles in protein function related to conformational plasticity, ligand binding, and sensing/mediating the effects of oxidative stress. A high degree of internal mobility, intrinsic detection sensitivity of the methyl group, and low copy number have made methionine labeling a popular approach for NMR investigation of selectively labeled protein macromolecules. However, selective labeling approaches are subject to more limited information content. In order to optimize the information available from such studies, we have performed DFT calculations on model systems to evaluate the conformational dependence of (3)J (CSCC), (3)J (CSCH), and the isotropic shielding, sigma(iso). Results have been compared with experimental data reported in the literatur

SUBMITTER: Butterfoss GL 

PROVIDER: S-EPMC5598763 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature