Towards Unveiling the Hidden Dynamics of Bacteriorhodopsin with Mems-Based Atomic Force Microscopy
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 high-sensitivity 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 time-resolved protein mechanics into the nanosecond regime.
Authors
- Guillaume Jourdan (ORCID: https://orcid.org/0000-0002-0944-8640)
- Bernard Legrand (ORCID: https://orcid.org/0000-0001-5158-3654)
- Ignacio Casuso (ORCID: https://orcid.org/0000-0001-7192-0136)
- Nicolas Mauran
- Shyamala Subramanian
Institutions
- Centre National de la Recherche Scientifique (FR)
- Université Fédérale de Toulouse Midi-Pyrénées (FR)
- Aix-Marseille Université (FR)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- CEA Grenoble (FR)
- Direction de la Recherche Technologique (FR)
- Dynamique du noyau (FR)
- Laboratoire d'Électronique des Technologies de l'Information (FR)
Publication Details
- Published
- 2025-06-29
- DOI
- https://doi.org/10.1109/transducers61432.2025.11110349
- Citations
- 1
- Primary Topic
- Photoreceptor and optogenetics research
- Type
- article
- Field-Weighted Citation Impact
- 0.91