Direct Observation of Millisecond to Second Motions in Proteins by Dipolar CODEX NMR Spectroscopy

摘要

The study of protein conformational dynamics is vitally important for the understanding of the molecular mechanisms underlying their biological function. Internal motions on the microsecond to second time scale are of particular interest, since this is the time scale of many biologically relevant events, such as catalysis, recognition, folding, etc. In solution, the exact NMR assessment of such slow motions is challenged by the overall Brownian tumbling that averages dipolar, chemical shift anisotropy (CSA), and quadrupolar interactions. In contrast, in the solid state, these interactions can be beneficially employed to access the whole frequency range of internal protein dynamics, along with a direct elucidation of the geometric details of molecular motions.