SUMMARY:

We perform high-resolution atomic force microscopy (AFM) imaging and force spectroscopy of membrane proteins. We are interested in "the structure and assembly of membrane proteins in native membranes studied by atomic force microscopy". Information concerning structure, function related conformational changes, and supramolecular assemblies, crucial for a complete understanding of a membrane protein, can be contributed by AFM. AFM experiments are performed in physiological buffer at room temperature and under normal pressure. The AFM features an outstanding signal-to-noise ratio allowing membrane proteins to be directly visualized in their native environment, the native membrane. Only in the native membrane can the native supramolecular assemblies, i.e. nanometric machines constituted of several membrane proteins working together, be observed. These supramolecular assemblies function in signal and energy transduction with impressiv efficiency. Recently, we could report high-resolution images of a photosynthetic membrane and its adaptation to different illumination.


FINANCING:

- Institut Curie
- INSERM
- INSERM Avenir Program 2005
- ANR PNANO-06-0089
- Ministere de Recherche France
- La medaille de la Ville de Paris - Projet en Recherche Medicale et en Sante
- Nanosciences Ile-de-France
- La Fondation Pierre-Gilles de Gennes
- ANR PCV-08-343399
- ANR PNANO-08

RESEARCH PROJECTS:

- Studying membrane protein assemblies in response to environmental factors
- High resolution AFM imaging of complex native membranes
- Force measurements describing the interactions between membrane proteins
- Development of novel AFM supports
- High-speed atomic force microscopy (HS-AFM)


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