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Univ. Paris-Saclay


Laboratoire Léon-Brillouin (LLB), Saclay, France

tel.jpg +33 1 69 08 67 20

CV : CV_SCombet_feb19.pdf


Staff scientist (CNRS) at the LLB, the French neutron source ;  instrument responsible of PACE SANS (small-angle neutron scattering) diffractometer.

Scientific activity

Coherent neutron scattering provides structural information in addition to, or instead of, the more classical structural methods used in structural biology (XR-crystallography, NMR, cryo-electron microscopy) in challenging situations such as protein assemblies or proteins in complex environments.

I use currently small-sangle neutron scattering (SANS) and specular neutron  reflectivity (SNR)  to probe:

  • the structure of proteins in interaction with different partners: polymers (hemoglobin/PEG blood substitute), lipids (dystrophin/muscle membrane ; prion/membrane interaction through the neurotoxic amyloid aggregation pathway), surfactants (TSPO channel membrane protein solubilized in detergents) or DNA (interaction of Ku protein and DNA and/or protein partners in the double-strand break repair pathway)
  • the influence of crowding or high pressure on protein structure and stability, especially on proteins of interest in food science (myoglobin, β-lactoglobulin, C-phycocyanin)

Publication list

Selected papers

Annighöfer B, Hélary A, Brûlet A, Colas de la Noue A, Loupiac C, Combet S. High pressure cell to investigate protein unfolding up to 600 MPa by small-angle neutron scattering. Rev Sci Instr, 90, 025106, 2019. DOI: 10.1063/1.5051765

Combet S, Cousin F, Rezaei H, Noinville S. Membrane interaction of off-pathway prion oligomers and lipid-induced on-pathway intermediates during prion conversion: a clue for neurotoxicity. Biochim Biophys Acta Biomembr 1861: 514, 2019. DOI: 10.1016/j.bbamem.2018.12.001

Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF. Human dystrophin structural changes upon binding to anionic membrane lipid. Biophys J 115: 1231, 2018. DOI: 10.1016/j.bpj.2018.07.039

Chevreuil M, Law-Hine D, Chen J, Bressanelli S, Combet S, Constantin D, Degrouard J, Möller J, Zeghal M, Tresset G. Nonequilibrium self-assembly dynamics of icosahedral viral capsids packaging genome or polyelectrolyte. Nature Comm 9: 3071, 2018. DOI: 10.1038/s41467-018-05426-8

Dos Santos Morais R, Delalande O, Pérez J, Mouret L, Bondon A, Martel A, Appavou MS, Le Rumeur E, Hubert JF, Combet S. Contrast-matched isotropic bicelles: a versatile tool to specifically probe the solution structure of peripheral membrane proteins using SANS. Langmuir 33: 6572-6580, 2017. DOI: 10.1021/acs.langmuir.7b01369

Le Coeur C, Combet S, Carrot G, Busch P, Teixeira J, Longeville S. Conformation of the polyethylene glycol chains in diPEGylated hemoglobin specifically probed by SANS: correlation with PEG length and in vivo efficiency. Langmuir 31: 8402-8410, 2015. DOI: 10.1021/acs.langmuir.5b01121

Combet S, Zanotti JM. Further evidence that hydration water is the main “driving force” of protein dynamics: a neutron scattering study on perdeuterated C-phycocyanin. Phys Chem Chem Phys 14: 4927-4934, 2012. DOI: 10.1039/c2cp23725c


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