Welcome to the Biophysics-Facility in the Faculty for Biology and Preclinical Medicine. We provide access and training to biophysical instruments allowing the characterization and quantification of molecular interactions, protein stability and size.?Detailed information on using the Facility can be found on the website of the L?ngst group (https://www.laengstlab.com/facilities/biophysics-facility/).

The facility offers instruments for MicroScale Thermophoresis (MST), Differential Scanning Fluorimetry (DSF) and Dynamic Light Scattering (DLS).

MicroScale Thermophoresis (MST) is an immobilization-free technology for measuring biomolecular interactions. The MST instrument detects the motion of fluorescent molecules along a microscopic temperature gradient, which reflects changes in the molecular hydration shell, charge, or size. Since one or all of these parameters will change with virtually every binding event, a wide range of biomolecules can be measured, from ions and small molecule fragments to large macromolecular complexes, in small volumes (~10 μl), in all kind of buffers and complex mixtures such as liposomes, detergent, serum, and cell lysates.

nanoDifferential Scanning Fluorimetry (nanoDSF) measures protein unfolding by monitory changes in fluorescence as a function of temperature. NanoDSF measures changes in intrinsic protein fluorescence as proteins unfold. Providing information about protein stability and the fraction of correct folded protein.

Dynamic Light Scattering (DLS) measures the time-dependent fluctuations in scattered light. These fluctuations are directly related to rate of diffusion of the molecule through the solvent, and can be used to measure hydrodynamic radius (Rh) of the particles in solution. ?????

Biolayer Inferometry (BLI)?is an optical technique that measures biomolecular interactions in real time. This label-free method eliminates the need for tags or dyes, preserving the natural behavior of your molecules.

BLI uses fiber-optical sensor tips, to which the biomolecules of interest are coupled. The sensor tips are then immersed in a solution containing a potential binding partner. When these molecules interact, they bind to the sensor, creating a change in the thickness of the biolayer on the sensor tip. This shift alters the interference pattern of white light reflected from the sensor surface, which is directly measured and translated into real-time kinetic data.”

Contact

Elisabeth Silberhorn
Mail: Elisabeth.Silberhorn@ur.de
Phone: 0941 9431848

Gernot L?ngst
Mail: Gernot.Laengst@ur.de
Phone: 0941 9432600