NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins.

ABSTRACT: Aromatic residues form a significant part of the protein core, where they make tight interactions with multiple surrounding side chains. Despite the dense packing of internal side chains, the aromatic rings of phenylalanine and tyrosine residues undergo 180° rotations, or flips, which are mediated by transient and large-scale "breathing" motions that generate sufficient void volume around the aromatic ring. Forty years after the seminal work by Wagner and Wüthrich, NMR studies of aromatic ring flips are now undergoing a renaissance as a powerful means of probing fundamental dynamic properties of proteins. Recent developments of improved NMR methods and isotope labeling schemes have enabled a number of advances in addressing the mechanisms and energetics of aromatic ring flips. The nature o

SUBMITTER: Akke M 

PROVIDER: S-EPMC9884080 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature