Solid-State NMR ¹⁹F-¹H-¹⁵N Correlation Experiments for Resonance Assignment and Distance Measurements of Multifluorinated Proteins.

ABSTRACT: Several solid-state NMR techniques have been introduced recently to measure nanometer distances involving ¹⁹F, whose high gyromagnetic ratio makes it a potent nuclear spin for structural investigation. These solid-state NMR techniques either use ¹⁹F correlation with ¹H or ¹³C to obtain qualitative interatomic contacts or use the rotational-echo double-resonance (REDOR) pulse sequence to measure quantitative distances. However, no NMR technique is yet available for disambiguating ¹H-¹⁹F distances in multiply fluorinated proteins and protein-ligand complexes. Here, we introduce a three-dimensional (3D) ¹⁹F-¹⁵N-¹H correlation experiment that resolves the distances of multiple fluorines to their

SUBMITTER: Duan P 

PROVIDER: S-EPMC10867861 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature