Introduction
The Molecular Biophysics Facility provides users with state of the art instruments along with expert data analysis. A comprehensive suite of tools enables in depth characterization of intrinsic properties of macromolecules and their assemblies (oligomeric states, aggregations, homogeneity, Mw, Rh) and biomolecular interactions (stoichiometry, affinity, thermodynamic and kinetic parameters). Facility scientists offer technical, methodological knowledge and expertise to help you tackle a range of biological questions and projects.
Protein stability and folding analysis
- Circular Dichroism (MOS500): provides information about folding and secondary structure of proteins.
- Fluorimeter (PTI QM4): produce insights from protein structure and conformational shifts.
- Thermal Shift Assay: identifies ligand binding, buffer conditions, and cofactors that influence protein stability.
Intrinsic properties of macromolecules and their assemblies
- Dynamic Light Scattering (DLS): determine the size (Rh) and aggregation of biological samples to assess homogeneity
- Nanoparticle Tracking Analysis (NTA): provides size distribution and concentration of large assemblies (LNP, exosomes).
- Mass Photometer (MPone): defines molecular mass and oligomerization status of proteins in their native state.
- Analytical Ultracentrifugation (AUC): analyses macromolecules sedimentation profiles to study macromolecular assemblies, aggregation and complex formation.
- SEC-MALS links size-exclusion chromatography (SEC) with multi-angle light scattering, refractive index, and UV-Vis detectors and DLS or viscometer for macromolecules characterisation.
Biomolecular interaction analysis
- BioLayer Interferometry (BLI): surface optics method used to characterize the kinetics of biomolecular interactions in real time and label free.
- Surface Plasmon Resonance (SPR ): surface optics method used to characterize the kinetics of biomolecular interactions in real time and label free.
- PEAQ-ITC: label free and solution method to measure binding parameters: affinity, thermodynamic parameters and stoichiometry.
- Microscale Thermophoresis (MST): quantifies macromolecular interactions from proteins movement in a temperature gradient.
Contact
biophysics.facility@ibs.fr
Facility staff:
Dr. Christine Chatellard
Aline Le Roy
Dr. Caroline Mas
Philippe Mas
Dr. Jean-Baptiste Reiser
Anne-Marie Villard
Facility Manager
Dr. Caroline Mas
Scientific expert
Dr. Christine Ebel
Access
The platform operates in two modes:
– The service mode (data acquisition with or without analysis)
– The provision of equipment for expert users after initial training.
Open to academic and private companies, depending on equipment and staff availability.
Costs
Samples
Only non-pathogenic biological samples are accepted. Decree of the July 18, 1994 establishing the list of biological pathogens, amended by Decrees of April 17, 1997 and June 30, 1998 (Decrees in French).
Sample requirements will be specified for each instrument on its dedicated webpage.
Results
In service mode:
Experiments and analysis are carried out by the platform: the time between experiments and report ranges from a few days to a few weeks.
The report is sent by Email, with raw data and related files.
In provision mode:
Each user analyse his results using the softwares on the instrument computer.
Data can be exported as text or excel files.
Each user should save his data and analysis after the experiments.
The user is responsible for definitive archiving.
Acknowledgements
Please find below the sentence that has to be written in all publications based on our UAR platforms:
« This work used the platforms of the Grenoble Instruct-ERIC center (ISBG ; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). We thank first name, surname (of all platform staff involved) for assistance and/or access to the biophysics platform. »
The platform staff is a co-author of the papers if he participates to redaction.
