Toward protein NMR at physiological concentrations by hyperpolarized water-Finding and mapping uncharted conformational spaces.

ABSTRACT: Nuclear magnetic resonance (NMR) spectroscopy is a key method for determining the structural dynamics of proteins in their native solution state. However, the low sensitivity of NMR typically necessitates nonphysiologically high sample concentrations, which often limit the relevance of the recorded data. We show how to use hyperpolarized water by dissolution dynamic nuclear polarization (DDNP) to acquire protein spectra at concentrations of 1 μM within seconds and with a high signal-to-noise ratio. The importance of approaching physiological concentrations is demonstrated for the vital MYC-associated factor X, which we show to switch conformations when diluted. While in vitro conditions lead to a population of the well-documented dimer, concentrations lowered by more than two orders of mag

SUBMITTER: Epasto LM 

PROVIDER: S-EPMC9355353 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature