Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional ¹H-detected solid-state NMR.

ABSTRACT: NMR chemical shifts provide detailed information on the chemical properties of molecules, thereby complementing structural data from techniques like X-ray crystallography and electron microscopy. Detailed analysis of protein NMR data, however, often hinges on comprehensive, site-specific assignment of backbone resonances, which becomes a bottleneck for molecular weights beyond 40 to 45 kDa. Here, we show that assignments for the (2x)72-kDa protein tryptophan synthase (665 amino acids per asymmetric unit) can be achieved via higher-dimensional, proton-detected, solid-state NMR using a single, 1-mg, uniformly labeled, microcrystalline sample. This framework grants access to atom-specific characterization of chemical properties and relaxation for the backbone and side chains, including those

SUBMITTER: Klein A 

PROVIDER: S-EPMC8795498 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature