Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary ¹⁵N and ¹H Relaxation Dispersion Techniques.

ABSTRACT: NMR relaxation dispersion methods provide a holistic way to observe microsecond time-scale protein backbone motion both in solution and in the solid state. Different nuclei (¹H and ¹⁵N) and different relaxation dispersion techniques (Bloch-McConnell and near-rotary-resonance) give complementary information about the amplitudes and time scales of the conformational dynamics and provide comprehensive insights into the mechanistic details of the structural rearrangements. In this paper, we exemplify the benefits of the combination of various solution- and solid-state relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain), for which we are able to identify and model the functionally relevant conformational rearrangements around the ligand reco

SUBMITTER: Rovo P 

PROVIDER: S-EPMC6982537 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature