Determination of Long-Range Distances by Fast Magic-Angle-Spinning Radiofrequency-Driven ¹⁹F-¹⁹F Dipolar Recoupling NMR.

ABSTRACT: Nanometer-range distances are important for restraining the three-dimensional structure and oligomeric assembly of proteins and other biological molecules. Solid-state NMR determination of protein structures typically utilizes ¹³C-¹³C and ¹³C-¹⁵N distance restraints, which can only be measured up to ∼7 Å because of the low gyromagnetic ratios of these nuclear spins. To extend the distance reach of NMR, one can harvest the power of ¹⁹F, whose large gyromagnetic ratio in principle allows distances up to 2 nm to be measured. However, ¹⁹F possesses large chemical shift anisotropies (CSAs) as well as large isotropic chemical shift dispersions, which pose challenges to dipolar coupling measurements. Here, we demonstrate ¹⁹

SUBMITTER: Roos M 

PROVIDER: S-EPMC6314681 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature