Characterization of biomolecular interactions using Microscale thermophoresis (MST) and Protein quality control using Tycho NT.6
Microscale Thermophoresis (MST) is a powerful method to determine affinities of all kinds of biomolecular interactions mainly driven by fluorescence changes and thermophoresis. It measures the motion of molecules along microscopic temperature gradients (temperature related intensity change, or TRIC, effect) and detects changes in their hydration shell, charge, or size, which allows for broad applications that range from small-molecule binding events to protein-protein interactions, and interactions of multi-protein complexes. With the flexibility and sensitivity of MST you have easier and faster access to Kd values. Moreover, the Tycho NT.6™, allows you to have more trustworthy, repeatable and consistent results to control the quality of your sample before each interaction measurement, or purification workflow, and thus allows you to conduct more detailed studies. The Tycho NT.6™ measures unfolding profiles due to the intrinsic fluorescence of proteins, along a temperature gradient. The presentation will focus on the description of these two technologies and some of their applications.
If you would like to meet the speaker after the seminar, please contact Mathilde.Belnou@nanotempertech.com
Technical Sales Specialist, NanoTemper Technologies GmbH, Munich, Germany
Application Specialist, NanoTemper Technologies GmbH, Munich, Germany
Domain 1 - UMR 9187 / U1196 - Chemistry, Modelling and Imaging for Biology