Biophysics of Macromolecules and their interactions

Presentation of the Platform

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), created in 2002, federates an ensemble of state-of-the-art instrumentation for the in vitro molecular-scale characterization of biological macromolecules, together with well-established technical and methodological expertise. This core facility, which is unique in France, provides a scientific environment conducive to world-class research in the field of macromolecular science.

The PFBMI presently comprises 8 technologies allowing to address questions concerning the study of intrinsic properties of macromolecules (folding, stability, auto-association, …) and of the interactions in which they are involved (stoichiometry, thermodynamic and kinetic parameters, …): analytical ultracentrifugation, circular dichroism, dynamic and static light scattering, viscometry, fluorescence and infra-red spectroscopies, microcalorimetry, and surface plasmon resonance.

 5 selected publications (2008-2010) :
1) A. Srivastava, S. Gangnard, A. Round, S. Dechavanne, A. Juillerat, B. Raynal, G. Faure, B. Baron, S. Ramboarina, S.K. Singh, H. Belrhali, P. England, A. Lewit-Bentley, A. Scherf,  G.A Bentley & B. Gamain (2010) “Full-length extracellular region of the var2CSA variant of PfEMP1 is required for specific, high-affinity binding to CSA”. PNAS, vol. 107, pp. 4884-4889.

2) I. Broutin, J-B. Jomain, E. Tallet, J. van Agthoven, B. Raynal, S. Hoos, B.B. Kragelund, P.A. Kelly, A. Ducruix, P. England & V. Goffin (2010)
"Crystal structure of an affinity-matured prolactin complexed to its dimerized receptor reveals the topology of hormone binding site 2".  J. Biol.  Chem., vol. 285, pp. 8422-8433.

3) P. England, A. Wehenkel, S. Martins, S. Hoos, G. André-Leroux, A. Villarino & P.M. Alzari (2009)
  "The FHA-containing protein GarA acts as a phosphorylation-dependent molecular
switch in mycobacterial signaling". FEBS Lett., vol. 583, pp. 301-307.

4) C. Tanous, O. Soutourina, B. Raynal, M.F. Hullo, P. Mervelet, A.M. Gilles, P. Noirot,  A. Danchin, P. England & I. Martin-Verstraete (2008)
  "The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis". J. Biol. Chem., vol. 283, pp. 33551-33560.

5) P. England, L.F. Westblade, G. Karimova, V. Robbe-Saule, F. Norel & A. Kolb (2008)
  "Binding of the unorthodox transcription activator, Crl, to the components of the transcription machinery". J. Biol. Chem., vol. 283, pp. 33455-33464.