Jean-Luc POPOT


Jean-Luc POPOT
's background is in biochemistry and biophysics, with a marked interest for physical chemistry. Since he entered research, his work has focused on integral membrane proteins, with two major types of research:


i) Understanding the structure and function of some specific proteins, mainly the nicotinic acetylcholine receptor, bacteriorhodopsin, the major proteolipid from myelin (PLP) and cytochrome b6f ;
ii) Developing general methods or concepts, applicable to most if not all integral membrane proteins, in particular understanding the mechanisms that determine the folding, assembly and stability of those membrane proteins whose transmembrane domain is made up of α-helices; exploring new methods of sequence analysis; and developing novel chemical tools for handling and/or studying membrane proteins, in particular two families of surfactants, fluorinated surfactants and amphiphilic polymers ('amphipols').

His current work focuses on developing amphipols and their applications.


Address:

Laboratoire de Biologie Physico-Chimique des Protéines Membranaires UMR 7099 - IBPC
13 rue Pierre et Marie Curie F-75005 Paris, France
Mail : jean-luc.popot(at)ibpc.fr
Lab Web page: http://www.ibpc.fr/UMR7099/
Personal Web page: http://www.ibpc.fr/popot/
Amphipol Web page: http://www.ibpc.fr/popot/amphipol/

Selected Articles:

  1. Popot, J.-L., Cartaud, J. & Changeux, J.-P. (1981). Reconstitution of a functional acetylcholine receptor: incorporation into artificial lipid vesicles and pharmacology of the agonist-controlled permeability changes. Eur. J. Biochem. 118, 203-214.
  2. Popot, J.-L., Gerchman, S.-E. & Engelman, D. M. (1987). Refolding of bacteriorhodopsin in lipid bilayers: a thermodynamically controlled two-stage process. J. Mol. Biol. 198, 655-676.
  3. Popot, J.-L., Pham-Dinh, D. & Dautigny, A. (1991). Major myelin proteolipid: the 4-α-helix topology. J. Membrane Biol. 120, 233-246.
  4. Pierre, Y., Breyton, C., Kramer, D. & Popot, J.-L. (1995). Purification and characterization of the cytochrome b6 f complex from Chlamydomonas reinhardtii. J. Biol. Chem. 270, 29342-29349.
  5. Tribet, C., Audebert, R. & Popot, J.-L. (1996). Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. Proc. Natl. Acad. Sci. USA 93, 15047-15050.
  6. Stroebel, D., Choquet, Y., Popot, J.-L. & Picot, D. (2003). An atypical haem in the cytochrome b6 f complex. Nature 426, 413-418.
  7. Breyton, C., Chabaud, E., Chaudier, Y., Pucci, B. & Popot, J.-L. (2004). Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions? FEBS Lett. 564, 312-318.
  8. Charvolin, D., Perez, J.-B., Rouvière, F., Giusti, F., Bazzacco, P., Abdine, A., Rappaport, F., Martinez, K. L. & Popot, J.-L. (2009). The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports. Proc. Natl. Acad. Sci. USA 106, 405-410.

Selected Reviews:

  1. Popot, J.-L. & Changeux, J.-P. (1984). Nicotinic receptor of acetylcholine: structure of an oligomeric integral membrane protein. Physiol. Rev. 64, 1162-1239.
  2. Popot, J.-L. & Engelman, D. M. (1990). Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29, 4031-4037.
  3. Popot, J.-L. (1993). Integral membrane protein structure: transmembrane α-helices as autonomous folding domains. Curr. Opin. Struct. Biol. 3, 532-540.
  4. Popot, J.-L. & Engelman, D. M. (2000). Helical membrane protein folding, stability and evolution. Annu. Rev. Biochem. 69, 881-923.
  5. Popot et al. (2003). Amphipols: polymeric surfactants for membrane biology research. Cell. Mol. Life Sci. 60, 1559-1574.
  6. Popot, J.-L. (2010). Amphipols, nanodiscs, and fluorinated surfactants: three non-conventional approaches to studying membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79, 737-775.
  7. Popot et al. (2011). Amphipols from A to Z. Annu. Rev. Biophys. 40, 379–408.