TOWARDS UNVEILING THE HIDDEN DYNAMICS OF BACTERIORHODOPSIN WITH MEMS-BASED ATOMIC FORCE MICROSCOPY
Résumé
Understanding membrane protein unfolding is essential for elucidating protein stability and function.
Here, we employ MEMS-based atomic force microscopy (AFM) to investigate the unfolding dynamics of bacteriorhodopsin (BR) with microsecond resolution. Compared to conventional cantilevers, High frequency MEMS probes minimize meniscus effects and enable highsensitivity force spectroscopy under dry conditions. Unfolding force-extension curves reveal discrete structural transitions consistent with BR domain unfolding. These findings demonstrate MEMS-AFM as a valuable tool for high-speed biomolecular force measurements. This study also lays the groundwork for implementing optomechanical probes at > 100 MHz, advancing timeresolved protein mechanics into the nanosecond regime.
| Origine | Fichiers produits par l'(les) auteur(s) |
|---|---|
| Licence |