Isothermal Titration Calorimetry
ITC200 and PEAQ-ITC resolve the complete thermodynamic profile of a binding event in solution — affinity, stoichiometry, enthalpy and entropy — without labels.
Interaction
Analytical Ultra Centrifugation
Beckman XLA (OPTIMA AUC) sediments a sample in free solution to reveal oligomeric state, size and shape, with no surface, column or label involved.
Surface Plasmon Resonance
Biacore T200 tracks a binding interaction in real time as it happens, resolving on- and off-rates as well as affinity, without labelling either partner.
Stability
Differential Scanning Calorimetry
PEAQ-DSC scans a protein through a temperature ramp to read its thermal stability and the full thermodynamics of unfolding — Tm, ΔH and ΔCp — directly from the heat of denaturation.
Differential Scanning Fluorimetry
NT.Plex, Tycho and PANTA read a protein's own tryptophan fluorescence as it unfolds, giving thermal and chemical stability from nanoliter volumes with no dye or label.
Dynamic Light Scattering
DLS Zetasizer reads a particle's size distribution and aggregation state straight from its light-scattering behaviour, with no separation step required.
Purification
Fast protein liquid chromatography
AKTA Pure purifies a protein by chromatography, resolving it from contaminants and aggregates by size, charge or affinity ahead of the biophysical assays that follow.
Lyophilisation
Purified samples are freeze-dried under vacuum, removing water by sublimation while preserving native structure for long-term storage and shipping.
Production
A construct is expressed in the system best matched to the target protein and purified to the quantity and purity a biophysical campaign requires.
Personnel
François Devred
Platform Director
Pascale Barbier
Analytical Ultracentrifugation
Géraldine Ferracci
Surface Plasmon Resonance
Philipp Tsvetkov
Molecular interactions Protein stability
Andréa Romette
Protein PurificationContact
PINT — Campus Timone
3rd floor, aile verte
Faculté de médecine
Aix-Marseille Université
