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Group leader: Simon Scheuring
Keywords: atomic force microscopy, membrane protein, membrane structure, supramolecular assembly Read the scientific activity report. (pdf 230Ko, last update 9th, february 2010) Around 30% of the open reading frames in the human genome encode membrane proteins, and this class of proteins is implicated in many of life's most important processes: signalling, energy transduction, metabolite transport, to name but a few. They are, therefore, the target of the majority of drugs used nowadays and defects in membrane protein function underlie directly or indirectly many pathologies. Our team studies the structure and assembly of membrane proteins in native membranes by high-resolution atomic force microscopy (AFM) imaging and force spectroscopy. One enormous advantage of AFM over other high-resolution imaging techniques is that it can be performed in physiological buffers at room temperature and under normal pressure. AFM measurements also have an outstanding signal-to-noise ratio. Together, these features allow us to visualise individual membrane proteins directly in their natural environment, the native membrane. Here, large supramolecular assemblies - nanomachines comprising several membrane proteins working together - can be observed by AFM to great effect. Supramolecular assemblies function in signal and energy transduction with impressive efficiency. Recently, we reported high-resolution images of a photosynthetic membrane (Fig. 1) and its adaptation to various levels of illumination as well as the supramolecular assembly of membrane proteins in junctional microdomains in the lens membranes of the eye (Fig. 2). We have also developed a two-chamber setup that allows a single membrane bilayer between two aqueous compartments to be imaged by AFM. We plan to develop AFM as a biomedical imaging and force probe tool. In the long term, we aim to perform high-resolution imaging of natural cytoplasmic membranes. Personal lab web page: perso.curie.fr/Simon.Scheuring Last update: February 2010 Key publications2009
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