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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Scientific Fields
Diseases
Organisms
Applications
Technique
Starting Date
20
Feb 2020
Status
Ongoing
Members
3
Structures
1

About

Equilibrium affinity constants (Kd) of protein-protein or protein-ligand interactions can be determined by performing  titrations, and monitoring  the extrinsic or intrinsic fluorescence of partners by Fluorescence spectroscopy (intensity or anisotropy) or by Microscale thermophoresis (LabelFree  or NT-115)

 

SPR (Biacore T200, GE Healthcare,) and BLI (OctetRed384, ForteBio) allow to monitor molecular interactions in real time, and to determine the rates of association (kon) and dissociation (koff) of biomolecular complexes

Isothermal microcalorimetry (VP-ITC and ITC200) enables the thermodynamic characterization of molecular interactions in solution (determination of reaction enthalpy and entropy)

Access Protocol

PFBMI equipments are available for all scientists worldwide, but a priority is given to members of Institut Pasteur and the Institut Pasteur International Network.
Requests can be submitted at any time  (biophysique@pasteur.fr) attaching a project submission form.