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 […]
This service allows you to obtain a full qualitative analysis (QC) of your purified proteins and helps you to identify conditions in which these proteins are best behaved. The basic analysis will provide you […]
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 […]
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 gives access to the […]
Analytical Ultracentrifugation gives access to the mass and shape of macromolecules in solution, allowing to evaluate their oligomerization state, their stoichiometry and the equilibrium constant of assemblies. Dynamic Light Scattering (cuvette or microplaque) allows […]
Static Light Scattering allows to measure the mass and intrinsic viscosity of macromolecules Analytical Ultracentrifugation gives access to the oligomerization state and the stoichiometry of molecular assemblies
Fluorescence spectroscopy is a versatile technique which allows to analyze, at steady-state or in real time, the variations of the environment of fluorescent probes, either intrinsic (for instance tryptophans in the case of proteins) […]
A Taylor dispersion instrument allows the determination of the diffusion coefficient, the hydrodynamic radius and the intrinsic viscosity of molecules. The method measures the dispersion of a solute pulse injected into a flowing fluid […]
Mass Photometry is offered using the Refeyn TwoMP system. This applies the principle of interference reflection microscopy and interferometric scattering microscopy to quantify light scattered by a single molecule on a glass surface. The […]
The PFBMI has a high-throughput non-microfluidic BLI instrument (Octet RED384, ForteBio) that enables the label-free analysis of 16 molecular interactions simultaneously in real time. To that avail, one of the interaction partners is immobilized […]
The PFBMI has a Optima (Beckman-Coulter) analytical ultracentrifuge with a dual UV/visible and interference detection system. The hydrodynamic behavior of a macromolecule and its sedimentation coefficient are determined by different parameters: volume, shape, density […]
Matrix-assisted laser desorption/ionization (MALDI) is a soft ionization processes due to its capacity to transfer a moderate excess of energy to the analyte, which is crucial for fragile and non-volatile compounds such as proteins. […]
NanoDSF measures the thermal denaturation of proteins by following the modification of the environment of their fluorescent aminoacids Tryptophanes and Tyrosines . Prometheus (Nanotemper) instrument can perform fast and sensitive simultaneous analyses of 48 […]
Fourier Transform Infra Red (FTIR) spectroscopy allows to analyze the secondary structure of macromolecules by measuring absorption frequencies of some specific chemical groups (notably, for proteins, that of the amide bond). Informations given by FTIR are […]
Studying the dynamic light scattering of particles in solution allows to quantify their diffusion coefficient and to deduce their hydrodynamic radius (which depends notably on their mass and shape). The PFBMI has a DynaPro […]
Microscale thermophoresis allows to monitor a great variety of molecular interactions rapidly and with a very low sample consumption, by measuring optically the mobility of macromolecules in a microscopic temperature gradient generated in a […]
Microcalorimetry enables the thermodynamic characterization of molecular interactions in solution, and of biochemical reactions in general. The Capillary Differential scanning calorimeter (CAP-DSC, Malvern) is principally dedicated to the study of the thermal stability of […]
Microcalorimetry enables the thermodynamic characterization of molecular interactions in solution, and of biochemical reactions in general. Isothermal titration calorimeters (VP-ITC et ITC200) are principally dedicated to the study of molecular interactions. By measuring the […]
The PFBMI has a ProteomeLab XL-I (Beckman-Coulter) analytical ultracentrifuge with a dual UV/visible and interference detection system. The hydrodynamic behavior of a macromolecule and its sedimentation coefficient are determined by different parameters: volume, shape, […]
Fluorescence spectroscopy is a versatile technique which allows to analyze, at steady-state or in real time, the variations of the environment of fluorescent probes, either intrinsic (for instance tryptophans in the case of proteins) […]
Fluorescence spectroscopy is a versatile technique which allows to analyze, at steady-state or in real time, the variations of the environment of fluorescent probes, either intrinsic (for instance tryptophans in the case of proteins) […]
Microscale thermophoresis allows to monitor a great variety of molecular interactions rapidly and with a very low sample consumption, by measuring optically the mobility of macromolecules in a microscopic temperature gradient generated in a […]
The PFBMI has a microfluidic SPR instrument (Biacore T200, Cytiva) that enables the label-free analysis of molecular interactions in real time. To that avail, one of the interaction partners is immobilized on a sensorchip, […]
Microcalorimetry enables the thermodynamic characterization of molecular interactions in solution, and of biochemical reactions in general. Isothermal titration calorimeters (VP-ITC et ITC200), principally dedicated to the study of molecular interactions. By measuring the reaction […]
The intensity of light scattered by a solution is directly proportional to the average molecular weight and to the concentration of its components. The PFBMI has a multiple detector (OMNISEC GPC/SEC, Malvern), coupled to […]
Studying the dynamic light scattering of particles in solution allows to quantify their diffusion coefficient and to deduce their hydrodynamic radius (which depends notably on their mass and shape). The PFBMI has a cuvette […]
The PFBMI has an J-1500/ 450W instrument. Studying macromolecules (and in particular proteins) by circular dichroism allows to obtain information about their folding. For proteins, far UV (180-260 nm) and near UV (250-330 nm) […]
