Abstract
Limited chemical shift dispersion represents a major barrier to studying multi-state equilibria of large membrane proteins by 19F NMR. We describe a novel monofluoroethyl 19F probe with a dramatically larger chemical shift dispersion than existing probes. The improved conformational sensitivity and line shape enabled the detection of hidden states of a critical membrane transporter, guiding subsequent structural elucidation by single-particle cryo-electron microscopy.
Competing Interest Statement
The authors have declared no competing interest.
Copyright
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
Posted March 30, 2022.
An environmentally ultrasensitive 19F NMR probe for monitoring protein conformational equilibria
