|Biophysics of Macromolecules and their Interactions - CNRS URA 2185|
|HEAD||Dr. Patrick ENGLAND / firstname.lastname@example.org|
|MEMBERS||Engineers: Bruno BARON, Sylviane HOOS , Bertrand RAYNAL
Secretary: Jocelyne FRAYSSE
Molecular-scale biophysical approaches are a privileged link between the atomic-level structural descriptions and the spatiotemporal in situ studies, providing invaluable information about the energetics and dynamics of biological macromolecules and assemblies in a relatively short time-scale and in close-to-physiological conditions.
The Centre of Biophysics of Macromolecules and their Interactions (french acronym: PFBMI) aims to group state-of-the-art equipment, adapted in priority to the needs of the research teams of the Pasteur Institute and its International Network, together with the corresponding technical and methodological know-how, thereby providing a scientific environment conducive to world-class research in the field of macromolecular science.
The following technologies are presently available (december 2007):
1) Analytical ultracentrifugation: ProteomeLab XL I & Optima XL-A ultracentrifuges (Beckman-Coulter).
2) Circular dichroism: Aviv 215 spectropolarimeter (Aviv Biomedical), with fluorescence and titration accessories ; CD6 spectropolarimeter (Jobin-Yvon) with a “stopped-flow” accessory (Bio-Logic).
3) Fluorescence spectroscopy: Quantamaster C60 fluorimeter (Photon Technology International), with a polarisation module ; KinetAsyst SF61-DX2 “stopped flow” instrument (Hi-Tech Scientific), with a polarisation module.
4) Infrared spectroscopy: MB104 spectrometer (ABB Bomem), with a DuraSamplIR II attenuated total reflectance accessory (SensIR).
5) Light scattering: DynaPro MS800 dynamic light scattering instrument (Wyatt) ; TDA 302 light scattering-intrinsic viscosity-refractive index triple detector array (Viscotek), coupled to a GPCmax size exclusion chromatography system.
6) Microcalorimetry: VP-ITC & MCS-ITC isothermal titration calorimeters ; VP-DSC differential scanning calorimeter, with a Pressure Perturbation Calorimetry accessory (PPC) (MicroCal).
7) Surface plasmon resonance: Biacore 2000 biosensor (Biacore).
People wishing to use the instruments of the PFBMI, or seeking expert advice related to these technologies, must send an e-mail to a centralized address, email@example.com . Instructions and down-loadable forms are available from our Web site, as a support for these applications, which can be made at any time.
Experiments can be carried out according to 3 different schemes: 1) instrument allocation after user training; 2) service provision; 3) scientific collaboration.
In the past 4 years, the 13 instruments and the know-how of the PFBMI have attracted more than 110 projects altogether, in association with 27 Research Units of the Pasteur Institute (from 9 out of 10 Scientific Departments) and 17 laboratories from other institutions (french or foreign), leading to 35 peer-reviewed publications.
Below is a very small sample of subjects covered by scientific collaborations and having lead to publications:
* Elucidation of the role of several post-translational modifications in the tethering of protein HP1 to histone tails (EMBO Rep. (2004) 5, 490-496)
* Characterization of the coupling between the trimerization of the rabies virus glycoprotein and its interaction with nerve growth factor receptor p75NTR (J. Gen. Virol. (2005) 86, 2543-2552)
* Determination of the effect of natural pathogenic mutations of the NF-κB modulator protein NEMO on its stability and oligomerization properties (J. Biol. Chem (2006) 281, 6334-6348)
* Study of the conformational changes induced by calcium in the RTX subdomain of Bordetella pertussis adenylate cyclase toxin (J. Biol. Chem (2006) 281, 16914-16926)
* Physico-chemical characterization of Sta1, a novel archaeal transcriptional activator (N.A.R. (2006) 34, 4837-4845)
* Study of the control of the expression of the Clostridium difficile toxin by the transcriptional regulator TcdC (Mol. Microbiol. (2007) 64, 1274–1288)
* Structural and thermodynamical characterization of the properties of prolactin receptor antagonists (J. Biol. Chem (2007) 282, 33118-33131)
Keywords: spectroscopy, hydrodynamic, thermodynamic, kinetic, protein, polysaccharide, nucleic acid, lipid
Jomain, JB; Tallet, E; Broutin, I; Hoos, S; Van Agthoven, J; Kelly, PA; Ducruix, A; Kragelund, BB; England, P & Goffin, V. , 2007, "Structural and thermodynamical bases for the design of pure prolactin receptor antagonists: X-ray structure of Del1-9-G129R-hPRL", Journal of Biological Chemistry 282, 33118-33131
Matamouros, S; England, P & Dupuy, B, 2007, "Clostridium difficile toxin expression is inhibited by the novel regulator TcdC", Molecular Microbiology64, 1274–1288
Villarino, A; Duran, R; Wehenkel, A; Fernandez, P; England, P; Brodin, P; Cole, ST; Zimny-Arnat, U; Jungblut, PR; Cerveñansky, C & Alzari, PM, 2005, "Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions", Journal of Molecular Biology350, 953–963
Mateescu, B; England, P; Halgand, F; Yaniv, M & Muchardt, C, 2004, “Tethering of HP1 proteins to chromatin is relieved by phosphoacetylation of histone H3”, b>EMBOReports5, 490-496
Merkulova-Rainon, T; England, P; Ding, SL; Demerens, C & Tobelem, R, 2003, “The N-terminal domain of hepatocyte growth factor inhibits the angiogenic behavior of endothelial cells independently from binding to the c-met receptor”, Journal of Biological Chemistry278, 37400-37408
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Activity Reports 2007 - Institut Pasteur
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