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Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by ¹⁹F NMR and Cryo-EM.

ABSTRACT: Limited chemical shift dispersion represents a significant barrier to studying multistate equilibria of large membrane proteins by ¹⁹F NMR. We describe a novel monofluoroethyl ¹⁹F probe that dramatically increases the chemical shift dispersion. The improved conformational sensitivity and line shape enable the detection of previously unresolved states in one-dimensional (1D) ¹⁹F NMR spectra of a 134 kDa membrane transporter. Changes in the populations of these states in response to ligand binding, mutations, and temperature correlate with population changes of distinct conformations in structural ensembles determined by single-particle cryo-electron microscopy (cryo-EM). Thus, ¹⁹F NMR can guide sample preparation to discover and visualize novel co

SUBMITTER: Huang Y

PROVIDER: S-EPMC10119980 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature

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Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by ¹⁹F NMR and Cryo-EM.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by ¹⁹F NMR and Cryo-EM.