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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)
FOR MORE INFORMATION SEE 'PUBLICATIONS' ON THE LEFT.
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