Mapping protein-protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy.

ABSTRACT: REDOR-based experiments with simultaneous ¹H-¹³C and ¹H-¹⁵N dipolar dephasing are explored for investigating intermolecular protein-protein interfaces in complexes formed by a U-¹³C,¹⁵N-labeled protein and its natural abundance binding partner. The application of a double-REDOR filter (dREDOR) results in a complete dephasing of proton magnetization in the U-¹³C,¹⁵N-enriched molecule while the proton magnetization of the unlabeled binding partner is not dephased. This retained proton magnetization is then transferred across the intermolecular interface by ¹H-¹³C or ¹H-¹⁵N cross polarization, permitting to establish the residues of the U-¹³C,^15</

SUBMITTER: Guo C 

PROVIDER: S-EPMC6258002 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature