Welcome to the Laboratory of Physical and Chemical Biology of Membrane Proteins

CNRS UMR 7099 - University Paris Diderot - Paris 7

Our laboratory gathers biologists, physicists and chemists who are interested in the structure, structural dynamics and physical chemistry of membrane proteins, either in vivo within a lipid bilayer, or in vitro after solubilization and stabilization by classical or alternative surfactants such as amphipols.

Our proteins of interest cover various domains of fundamental and medical biology:

  • Energy coupling & supramolecular organization of respiratory chain complexes with the structure-function study of the cytochrome b6f complex and the mitochondrial uncoupling proteins.
  • Molecular Signalization Pathway of GPGRs with the study of HEDGEHOG Pathway, the study of Signal Transduction by GPCRs using liquid state NMR and GPCR Cristallization.
  • Transport and Membrane Dynamics in Bacteria including the biochemistry of Iron Transport in Haemophilus, the membrane biogenesis in E. coli, solid state NMR of membranes and membrane proteins and the study of efflux pumps in bacteria.

In addition, all members of the unit contribute to the development of our tool box for membrane proteins studies, which includes: NMR, mass spectrometry, crystallography, physical-chemistry of surfactants, membrane protein production and synthetic biology.

Bruno Miroux

Head of unit


Third cycle teaching module
Protéines membranaires, structures, fonctions et implications en santé humaine

---From 19th to 21th June 2017---
More details and Program.

Second Structural Biochemistry Course
---From 23th to 30th March 2017---
More details and Program.


RMN-Ile de France Workshop,
Tuesday April 25th, 2016, IBPC, Paris (FRANCE)
more details and program.

Membranes & Molecules Seminars

Ian Collinson
(Tuesday, March 28th 2017, 11h30)
University of Bristol, School of Biochemistry, UK
Mechanism of protein secretion and membrane protein insertion through the bacterial translocon (abstract)

PhD defense

Staëlle Makamté , March 20th 2017

Recently published

H.Y. Fu, D. Picot, Y. Choquet, G. Longatte, A. Sayegh, J. Delacotte, M. Guille-Collignon, F. Lemaître, F. Rappaport & F.A. Wollman Redesigning the QA binding site of Photosystem II allows reduction of exogenous quinones. Nat Commun 8:15274 (2017) DOI: 10.1038/ncomms15274 (Pubmed)

Job position

No position available for the moment.

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Last update: 17/04/26

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