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Présentation Membrane Proteins In Aqueous Solutions de Popot, Jean - Luc Format Broché
- Livre Physique - Chimie
Résumé : Jean-Luc Popot, born 1948, studied biology, chemistry, and biophysics in Orl?ans and Orsay. In 1971, he took a permanent position with the Coll?ge de France. In J.?P. Changeux's laboratory, at the Pasteur Institute, he applied electrophysiology and biophysical and biochemical approaches to functional and structural studies of the nicotinic acetylcholine receptor. In 1982, he joined D.M. Engelman at Yale University as a visiting scientist. His work at Yale, which bore principally on refolding bacteriorhodopsin from denatured fragments and studying the refolded structure crystallographically, led the two of them to propose, in 1990, an influential model for the folding of???helical membrane proteins. In 1985, he joined the laboratory of P. Joliot at the Institut de Biologie Physico-Chimique (Paris). His group carried out neutron diffraction and model building work on bacteriorhodopsin and biochemical studies on Photosystem?II and cytochrome b6?f . In 1996, he became Research Director at the Centre National de la Recherche Scientifique and created his own laboratory, where the X?ray structure of the was solved in 2003. In parallel, he pursued the development of sequence analysis approaches and, in collaboration with chemists and physical chemists, designed and validated non-conventional surfactants aimed at facilitating membrane protein solution studies, most notably amphipathic polymers ('amphipols') and fluorinated surfactants. He retired in 2013 and, along with his wife, splits his time between restoring an old house in Languedoc, reading, writing, hiking, photographing, cooking, and enjoying the company of kith and kin.
Biographie:
Jean-Luc Popot, born 1948, studied biology, chemistry, and biophysics in Orl?ans and Orsay. In 1971, he took a permanent position with the Coll?ge de France. In J.?P. Changeux's laboratory, at the Pasteur Institute, he applied electrophysiology and biophysical and biochemical approaches to functional and structural studies of the nicotinic acetyl?cho?li?ne receptor. In 1982, he joined D.M. Engelman at Yale University as a visiting scientist. His work at Yale, which bore princi?pal?ly on refolding bacterio?rhod?opsin from dena?tu?red fragments and studying the refolded structure crystallographically, led the two of them to propose, in 1990, an influential model for the folding of ??helical membrane proteins. In 1985, he joined the laboratory of P. Joliot at the Institut de Biologie Physico-Chimique (Paris). His group car?ried out neutron diffraction and model building work on bacterio?rhod?opsin and bio?che?mical studies on Photo?sys?tem II and cytochrome b6 f. In 1996, he became Research Director at the Centre National de la Recher??che Scienti?fi?que and created his own laboratory, where the X?ray struc?tu?re of the b6 f was solved in 2003. In parallel, he pursued the development of sequence analysis approa?ches and, in collabo?ra?tion with chemists and physical chemists, designed and validated non-conventional surfact?ants aimed at facilitating membrane protein solu?tion studies, most notably amphi??pathic polymers ('amphipols') and fluorinated surfactants. He retired in 2013 and, along with his wife, splits his time between restoring an old house in Languedoc, reading, writing, hiking, photographing, cooking, and enjoying the company of kith and kin....
Sommaire:
From the Contents: Membrane proteins: functions, structures, environments.- Taking membrane proteins out of their natural environment.- Alternatives to detergents for handling membrane proteins in aqueous solutions.- Chemical structure and physical-chemical properties of amphipols.
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