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Molecular Biophysics Platform (PFBMI)
Hosting Legal Entity
Institut Pasteur
25-28 rue du Docteur Roux, Paris, PO: 75015 (France)
25 rue du Docteur Roux, Institut Pasteur, Paris, PO: 75015 (France)
Type Of RI
Coordinating Country
Current Status:
Operational since 2002
Scientific Description
PFBMI, created in 2002 by Dr. Patrick England, is situated at the Institut Pasteur (Paris, France), and is recognized as a National core facility by the French IBISA consortium. It is open to all the scientific community, both academic and industrial, in France and abroad, through a transparent application process. It is the coordinating node of the large European molecular-scale biophysics network ARBRE-MOBIEU (funded by COST from 2016 to 2020). PFBMI federates a state-of-the-art ensemble of 20 instruments for the in vitro molecular-scale characterization of biological macromolecules, together with well-established technical and methodological expertise. The mission of the PFBMI is to provide an added value to a great variety of biological projects, enabling the characterisation of the intrinsic properties of macromolecules and their assemblies (size, shape, folding, stability, auto-association, …) and of the interactions in which they are involved (stoichiometry, thermodynamic and kinetic parameters, …).

RI Keywords
Molecular hydrodynamics, Molecular interactions, Biophysics, Molecular spectroscopy
RI Category
Biological/Biomedical Engineering and Biotechnology/Nanotechnology Research Facilities
Analytical Facilities
Structural Biology Facilities
Scientific Domain
Biological and Medical Sciences
ESFRI Domain
Health and Food
Macromolecular architecture, size and shape characterization

Determination of the oligomeric architecture, and of the size and shape of macromolecular assemblies

Secondary and tertiary structures of macromolecules

Circular dichroism (CD), allows the measurement of secondary and tertiary structures, the analyse of conformational changes, the kinetic of folding and the thermal and chemical stability of folding.Fluorescence spectroscopy give access to the analysis of tertiary conformation, of thermal and chemical stability and of molecular interactions through the measure of fluorescence intensity, anisotropy and life-time. Infrared spectroscopy (FTIR) allows the measurement of secondary structures of macromolecules, specially proteins with high content in ß sheath.

Thermodynamical stability of macromolecules

Circular dichroism (CD) spectroscopy allows the determination of secondary and tertiary structures, the analysis of conformational changes and the measure of thermal and chemical stability of folding.Differential Scanning Calorimetry (DSC) gives access to the thermal stability of macromolecules and their complexes.

AVIV 215

Access Type
Remote, Physical
Access Mode
Excellence Driven, Wide
Access Webpage
Users Definition
Teams of individual researchers
Date of last update: 20/05/2019
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