Structure-function properties in membrane proteins

People working with me on this project at CRMN: C. Ollier (PhD student), Z. Sun (post-doc), S. Medina-Gomez (post-doc), T. Le Marchand (IR CNRS), L. Pinet (MdC ENS Lyon).

Collaborators: Dr. R. Wagner (Univ. Strasbourg, FR), Dr. J. Sturgis (Aix-Marseille Univ., FR), Dr. J. Thoma, Pr. R. Burman and Pr. G. Karlsson (Univ. Goteborg), Pr. V. Ladizhansky (Univ. Guelph, CA), Pr. L. Arleth (U. Copehnagen, DK), Pr. B. Chmelka (UC Santa Barbara, CA), Pr. R. G. Griffin (MIT, MA).

The study of membrane proteins is particularly challenging due to their inherent structural disorder over long distances and restricted mobility within lipid bilayers. This disorder and limited motion make diffraction studies nearly impossible, while also causing significant broadening of NMR signals from different protein regions, which limits conventional solution NMR analyses.
Current targets in our lab include outer membrane pores of K. pneumoniae (e.g., OmpA), proteorhodopsin, the E. coli outer membrane protein OmpG, the alkane transporter AlkL from P. putida, a bacterial MgII/CoII transporter, and the highly medically relevant human metalloprotein hCTR1 involved in copper transport.

See: Saurel et al. J Am Chem Soc 2017, 139, 1590; Lalli et al. J Am Chem Soc 2017, 139, 13006; Retel et al. Nat Commun 2018, 8, 2073; Schubeis et al. Proc Natl Acad Sci USA 2020, 117, 21014; Bonaccorsi et al. Elife 2022, 11, e71887.