A novel high-dimensional NMR experiment for resolving protein backbone dihedral angle ambiguities.

ABSTRACT: Intrinsically disordered proteins (IDPs) are challenging established structural biology perception and urge a reassessment of the conventional understanding of the subtle interplay between protein structure and dynamics. Due to their importance in eukaryotic life and central role in protein interaction networks, IDP research is a fascinating and highly relevant research area in which NMR spectroscopy is destined to be a key player. The flexible nature of IDPs, as a result of the sampling of a vast conformational space, however, poses a tremendous scientific challenge, both technically and theoretically. Pronounced signal averaging results in narrow signal dispersion and requires higher dimensionality NMR techniques. Moreover, a fundamental problem in the structural characterization of IDPs

SUBMITTER: Kauffmann C 

PROVIDER: S-EPMC7211790 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature