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.
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.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.
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5 selected publications (2008-2010) :
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.