Rapid measurement of long-range distances in proteins by multidimensional ¹³C-¹⁹F REDOR NMR under fast magic-angle spinning.

ABSTRACT: The ability to simultaneously measure many long-range distances is critical to efficient and accurate determination of protein structures by solid-state NMR (SSNMR). So far, the most common distance constraints for proteins are ¹³C-¹⁵N distances, which are usually measured using the rotational-echo double-resonance (REDOR) technique. However, these measurements are restricted to distances of up to ~ 5 Å due to the low gyromagnetic ratios of ¹⁵N and ¹³C. Here we present a robust 2D ¹³C-¹⁹F REDOR experiment to measure multiple distances to ~ 10 Å. The technique targets proteins that contain a small number of recombinantly or synthetically incorporated fluorines. The ¹³C-¹⁹F REDOR sequence is combined with

SUBMITTER: Shcherbakov AA 

PROVIDER: S-EPMC6314655 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature