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.- Formation and properties of membrane protein/amphipol complexes.- Amphipol-assisted folding of membrane proteins to their native state.- Amphipol-assisted cell-free expression of membrane proteins.- Amphipols and NMR.- Amphipols and crystallography.- Amphipols and electron microscopy.- Amphipols and radiation scattering.- Amphipol-assisted immobilization of membrane proteins onto solid supports for ligand-binding studies.- Amphipols and proteomics.- Amphipols as vectors for the delivery of membrane proteins and transmembrane peptides.- Perspectives.- Annex: protocols.- Trapping membrane proteins with amphipols.- Amphipol-assisted folding of membrane proteins.- Amphipol-assisted cell-free expression of membrane proteins.- Preparing membrane protein/amphipol complexes for solution NMR.- Preparing membrane protein/amphipol complexes for electron microscopy.- Amphipol-assisted transfer of membrane proteins to lipid phases for crystallization.- Preparing membrane protein/amphipol complexes for radiation scattering measurements.- Using tagged amphipols to immobilize membrane proteins onto solid supports.- Preparing membrane protein/amphipol complexes for mass spectrometry.- Using membrane protein/amphipol complexes for vaccination.- Glossary.- Index.- Literature cited.

Jean-Luc Popot, born 1948, studied biology, chemistry, and biophysics in Orléans and Orsay. In 1971, he took a permanent position with the Collège 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 α-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.