06/01-2020 - Mathilde Belnou : Characterization of biomolecular interactions using MicroScale thermophoresis (MST) and quality control using Tycho NT.6™

06 - Janvier - 2020

LES LUNDIS DE SAINT-ANTOINE

Bâtiment Kourilsky - 13h–14h

Salle des Conférences (Rez de Chaussée),

184 rue du Faubourg Saint-Antoine, Paris

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LUNDI 06 JANVIER 2020

Characterization of biomolecular interactions using MicroScale thermophoresis (MST) and quality control using Tycho NT.6™

Mathilde Belnou

1NanoTemper Technologies GmbH, Munich, Germany

Invitée par Anne STARY Equipe HOUSSET

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Microscale Thermophoresis (MST) is a powerful method to determine affinities of all kinds of biomolecular interactions mainly driven by fluorescence changes (TRIC effect) and thermophoresis. It measures the motion of molecules along microscopic temperature gradients and detects changes in their hydration shell, charge or size allowing broad applications range from small-molecule binding events to protein-protein interactions and interactions of multi-protein complexes. With the flexibility and sensitivity of MST you could access easier and faster to the strength of the interaction by determining a Kd (Figure 1). Moreover, to go deeper in your projects and thanks to the Tycho NT.6™, you could have more trusty, repeatable and consistent results to control the quality of your sample, before each interaction measurements or purification workflow, for instance. It measures unfolding profiles due to intrinsic fluorescence of proteins, along a temperature gradient. The presentation will focus on description of these two technologies and provide you some applications.

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