Including Protons in Solid-State NMR Resonance Assignment and Secondary Structure Analysis: The Example of RNA Polymerase II Subunits Rpo4/7.

ABSTRACT: ¹H-detected solid-state NMR experiments feasible at fast magic-angle spinning (MAS) frequencies allow accessing ¹H chemical shifts of proteins in solids, which enables their interpretation in terms of secondary structure. Here we present ¹H and ¹³C-detected NMR spectra of the RNA polymerase subunit Rpo7 in complex with unlabeled Rpo4 and use the ¹³C, ¹⁵N, and ¹H chemical-shift values deduced from them to study the secondary structure of the protein in comparison to a known crystal structure. We applied the automated resonance assignment approach FLYA including ¹H-detected solid-state NMR spectra and show its success in comparison to manual spectral assignment. Our results show that reasonably reliable s

SUBMITTER: Torosyan A 

PROVIDER: S-EPMC6787281 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature