- Facility
Biophysics & Structural Biology (B2S)
- Microcalorimetry, Circular Dichroïsm, Surface Plasmon Resonance, NMR, Chromatography, Light Scattering, X-ray Cristallography, Fast kinetics, Cryomicroscopy
The Biophysics and Structural Biology (B2S) platform offers a combination of equipment for in vitro physicochemical characterization of proteins and interactions. It provides access to several biophysical (circular dichroism, microcalorimetry, surface plasmon resonance, fluorescence) and structural biology (NMR, X-ray) devices, and is based on the skills of the IMoPA research teams. It belongs to the ARBRE association (Association of Resources for Biophysical Research in Europe) created in 2015. It allows the development of multidisciplinary projects to characterize 1) the interactions involved between biological macromolecules and, 2) the 3D structure biological macromolecules.
The B2S staff has a real technical and methodological expertise to address different issues: The stability / characterization of proteins and complexes in solution, the three-dimensional structure of proteins and complexes, fast kinetics, the characterization of protein-protein and protein-ligand interactions as well as the isolation and characterization of a broad spectrum of products by liquid chromatography.
The platform operates in two modes: 1) the service mode (turnkey services along with, or not, collaborations) and 2) the provision of devices for expert users after initial training.
- Request form90.91 KBTerms and conditions319.06 KB
Any new collaborator must contact the person in charge of the Core Facility to define the best strategy to adopt for the project and complete the service request form. Any user will accept the terms and conditions for service use by signing the agreement form.
We are always available for users during the use of the devices and for any advice and assistance.
Each user must retrieve its data at the end of the analyses. In the usual case, the raw acquisition data are kept for 1 year on computer stations. The platform does not guarantee the recovery of data in case of malfunction. The user is responsible for the final data storage.
Chagot ME, Quinternet M, Jacquemin C, Manival X, Gardiennet C. Box C/D snoRNPs: solid-state NMR fingerprint of an early-stage 50 kDa assembly intermediate. Biomol NMR Assign. 2020 Feb 6.
10.1007/s12104-020-09933-y , 
32030621 , 
HAL-02480749 Dreyer A, Schackmann A, Kriznik A, Chibani K, Wesemann C, Vogelsang L, Beyer A, Dietz KJ. Thiol Redox Regulation of Plant β-Carbonic Anhydrase. Biomolecules. 2020 Jul 30.
10.3390/biom10081125 ,
32751472 ,
HAL-02917419 Albe Slabi S, Mathe C, Basselin M, Fournier F, Aymes A, Bianeis M, Galet O, Kapel R. Optimization of sunflower albumin extraction from oleaginous meal and characterization of their structure and properties. Food Hydrocolloids, Volume 99, 2020 Feb, 105335.
10.1016/j.foodhyd.2019.105335 - Risser F, Collin S, Dos Santos-Morais R, Gruez A, Chagot B, Weissman KJ. Towards improved understanding of intersubunit interactions in modular polyketide biosynthesis: docking in the enacyloxin IIa polyketide synthase. J Struct Biol. 2020 Jul 25.
10.1016/j.jsb.2020.107581 ,
32717326
Roret T, Alloing G, Girardet JM, Perrot T, Dhalleine T, Couturier J, Frendo P, Didierjean C, Rouhier N. Sinorhizobium meliloti YrbA binds divalent metal cations using two conserved histidines. Biosci Rep. 2020 Oct 30 ; 40(10):BSR20202956.
10.1042/BSR20202956 ,
32970113 Rzeigui M, Traikia M, Jouffret L, Kriznik A, Khiari J, Roy O, Taillefumier C. Strengthening Peptoid Helicity through Sequence Site-Specific Positioning of Amide Cis-Inducing NtBu monomers. J Org Chem. 2019 Dec 24.
10.1021/acs.joc.9b02916 ,
31873018 ,
HAL-02430577 Ioannou I, Kriznik A, Chekir L, Ghoul M. Effect of the Processing Temperature on the Degradation of Food Flavonoids: Kinetic and Calorimetric Studies on Model Solutions. J. Food Eng. and Technol. 2019 ; 8(2):91-102.
10.32732/jfet.2019.8.2.91 ,
HAL-02392716 Chagot ME, Dos Santos Morais R, Dermouche S, Lefebvre D, Manival X, Chipot C, Dehez F, Quinternet M. Binding properties of the quaternary assembly protein SPAG1. Biochem J. 2019 May 22.
10.1042/BCJ20190198 ,
31118266 ,
HAL-02140524 S Ahmed Zennia S, Mati A, Charron C, Cakir-Kiefer C, Kriznik A, Girardet JM. Effect of nonenzymatic deamidation on the structure stability of Camelus dromedarius alpha-lactalbumin.Food Chemistry. 2019 Avril 8.
10.1016/j.foodchem.2019.04.033 ,
HAL-02095313 Chagot ME, Quinternet M, Rothé B, Charpentier B, Coutant J, Manival X, Lebars I. The yeast C/D box snoRNA U14 adopts a "weak" K-turn like conformation recognized by the Snu13 core protein in solution. Biochimie. 2019 Mar 23.
10.1016/j.biochi.2019.03.014 ,
30914254 ,
HAL-02082477
