IBiSA Biophysical Chemistry Platform

  • Biomolecular interactions
  • Proteomics
  • Structural Biology
NFX 50-900 (ISO9001 for research lab) in 2015
Localization
Institut Européen de Chimie et Biologie (IECB) UMS3033/US001
DEMANDE D'UTILISATION

Contact

Description

The role of the SBPCP is to be at the forefront of methodological developments in Structural Biochemistry and Biophysics. At the SBPCP-IECB, molecular recognition and supramolecular assemblies are investigated from a structural and biophysical perspectives by regrouping expertises in NMR spectroscopy, X-ray crystallography (including SAXS/WAXS), molecular modeling, mass spectrometry, surface plasmon resonance and spectroscopy (absorption and circular dichroism spectroscopy).

Activity

  • NMR (solid and liquid state): structure determination from small molecules to large biomolecules and assemblies (instrument access time, notably via the TGIR, routine services and collaborative projects).
  • Mass spectrometry: mass measurements for verification/confirmation of compounds (instrument access time or routine services) and study of non-covalent assemblies (collaborative projects, operational since January 2013).
  • Crystallogenesis and X-ray diffraction/diffusion: structure determination, high throughput crystallization, SAXS/WAXS (mainly collaborative projects, two robotic devices for crystallization in access time).
  • Circular dichroism (instrument access time).
  • Surface plasmon resonance: kinetics/thermodynamics of interactions (mainly collaborative projects).
  • Electronic microscopy (mainly instrument access time). Molecular modeling (computer access time and collaborative projects).

Infrastructure and equipment

  • High field NMR (up to 800MhZ)
  • SPR, ITC, DSC, CD.
  • X-ray diffraction – SAXS – automatic cristallogenesis
  • Mass spectrometry (Ionic mobility)
  • High resolution Electron Microscopy

Publication

  1. Fremaux J, Mauran L, Pulka-Ziach K, Kauffmann B, Odaert B, Guichard G. α-Peptide-Oligourea Chimeras: Stabilization of Short α-Helices by Non-Peptide Helical Foldamers. Angew Chem Int Ed Engl. 2015 Aug 17;54(34):9816-20.
  2. Chandramouli N, Ferrand Y, Lautrette G, Kauffmann B, Mackereth CD, Laguerre M, Dubreuil D, Huc I. Iterative design of a helically folded aromatic oligoamide sequence for the selective encapsulation of fructose. Nat Chem. 2015 Apr;7(4):334-41.
  3. Mandal PK, Collie GW, Kauffmann B, Huc I. Racemic DNA crystallography. Angew Chem Int Ed Engl. 2014 Dec 22;53(52):14424-7.
  4. Sebaoun L, Maurizot V, Granier T, Kauffmann B, Huc I. Aromatic oligoamide β-sheet foldamers. J Am Chem Soc. 2014 Feb 5;136(5):2168-74.
  5. Gan Q, Ferrand Y, Bao C, Kauffmann B, Grélard A, Jiang H, Huc I. Helix-rod host-guest complexes with shuttling rates much faster than disassembly. Science. 2011 Mar 4;331(6021):1172-5
  6. Sanchez JF, Kauffmann B, Grélard A, Sanchez C, Trézéguet V, Huc I, Lauquin GJ. Unambiguous structure of atractyloside and carboxyatractyloside. Bioorg Med Chem Lett. 2012 Apr 15;22(8):2973-5.

Collaboration

  • Prof Kazushi Kinbara.  Tohoku University (Solid state NMR)
  • Prof Roland SIGEL. Department of Chemistry, University of Zurich MS: Mass spectrometry determination of the molecularity of NRAS RNA sequence
  • Prof Zwickler Jeff U. Harvard, Boston M (Electron microscopy)
  • Prof Apurba Das. Indian Institute of Technology Indore (X-ray Diffraction of peptides and SAXS on fibers)
  • Prof Marcelo Guerin.  Structural Glycobiology Group Leader, CSIC-UPV/EHU, Spain. SPR project on protein-ligand interactions.
Institut Européen de Chimie et Biologie (IECB) UMS3033/US001