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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

About

I am working on the Molecular Biophysics platform (PFBMI) (see https://research.pasteur.fr/en/team/biophysics/). 

I have set up a new service that allows you to obtain a full qualitative analysis (QC) of your purified proteins and to help you to identify conditions in which these proteins are best behaved.

The first level will provide you with information about the purity, identity, integrity and homogeneity of your protein. We will thus conduct a set of measurements composed of a mass spectrum, a UV/Visible spectrum and a DLS measurement.

If needed, we can also provide an electrophoresis profile and a SEC chromatogram of your sample.

Furthermore, buffer optimisation can also be performed: the stability and the solubility of protein samples can be tested in several buffers with various pH and salt compositions. Sample storage conditions can also be assessed as well as “lot to lot” reproducibility tests.

For more information, please send an email to qcprotein@pasteur.fr

The second goal of my work is the study of biomolecular hydrodynamics in order to obtain information about the mass, size, shape and architecture of the molecules of interest and their assemblies. On the PFBMI, we address hydrodynamic questions using analytical ultracentrifugation (AUC) in sedimentation velocity and equilibrium modes. With AUC, we can determine the oligomerization state of macromolecules and understand their interactions. For more information, please send an email to biophysique@pasteur.fr

 

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