Carbon-nitrogen REDOR to identify ms-timescale mobility in proteins.

ABSTRACT: Protein dynamics play key mechanistic roles but are difficult to measure in large proteins and protein complexes. INEPT and CP solid-state NMR experiments have often been used to obtain spectra of protein regions that are mobile and rigid, respectively, on the nanosecond timescale. To complement this approach, we have implemented ¹³C{¹⁵N} REDOR to detect protein regions with backbone dynamics on the millisecond time scale that average the ≈1 kHz carbon-nitrogen dipolar coupling. REDOR-filtering of carbon correlation spectra removes signals from rigid backbone carbons and retains signals from backbone carbons with ms-timescale dynamics that would be missing in dipolar-driven NCA/NCO spectra. We use these experiments to investigate functionally important dynamics within

SUBMITTER: Kashefi M 

PROVIDER: S-EPMC6656615 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature