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Integrated Structural Biology Grenoble

Contact person(s) related to this article / Caroline Mas

Microscale Thermophoresis

Definition

Microscale Thermophoresis is a method to quantify biomolecular interactions. It measures the motion of molecules along microscopic temperature gradients and detects changes in their hydration shell, charge or size. By combining the fluorescence detection with thermophoresis, MST provides a way to measure molecular interactions.

Principle

When performing a MST experiment, a microscopic temperature gradient is induced by an IR laser, and the movement of molecules is detected and quantified using either covalently attached dyes, fluorescent fusion proteins or intrinsic tryptophan fluorescence.

Microscale Thermophoresis Principle

Applications

The applications range from small-molecule binding events to protein-protein interactions and interactions of multi-protein complexes.

Staff

Platform engineer: Caroline Mas
Office: CIBB room 020
Instrument location: EMBL room 152

Instrument

Nanotemper Monolith NT.115

Manual NT.115
MST Starting guide

Location

The MST Monolith NT.115 is located at the EMBL, laboratory 152, 1st Floor (Map Here)

Access mode

  • Use of this instrument is for PSB users only.
  • There is no charge, but users must supply their own capillaries and labelling reagents.

How to make a request

To make a booking request, fill this REQUEST FORM HERE
You can also access to the booking system on the PSB website

MST Monolith NT.115 Booking

Follow up / acknowledgements

Acknowledgements in publications:
Please find below the sentence that has to be written in all publications based on our UMS platforms:
"This work used the platforms of the Grenoble Instruct-ERIC Center (ISBG : UMS 3518 CNRS-CEA-UGA-EMBL) with support from FRISBI (ANR-10-INBS-05-02) and GRAL (ANR-10-LABX-49-01) within the Grenoble Partnership for Structural Biology (PSB). We thank Caroline Mas and/or Marc Jamin, for assistance and/or access to the Biophysical platform."