Dresden 2011 – scientific programme

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CPP: Fachverband Chemische Physik und Polymerphysik

CPP 29: Biopolymers and Biomaterials III (jointly with BP)

CPP 29.9: Talk

Wednesday, March 16, 2011, 17:15–17:30, ZEU 260

Thermophoresis quantifies the Conformation and Stability of Biomolecules — •Christoph Jens Wienken, Philipp Baaske, Stefan Duhr, and Dieter Braun — Systems Biophysics, LMU München, Germany

Stability and conformation of biomolecules is important in the field of biology, medical diagnostics and biotechnology. We developed a method which measures both parameters using Microscale Thermophoresis, an all-optical technique which only uses 250nl of sample. Thermophoresis is the directed movement of molecules in a temperature gradient. It depends on surface characteristics of the molecule, such as size, charge and hydrophobicity [1]. Its sensitivity for small changes in above parameters was recently shown by analyzing the binding reactions of DNA aptamers and a variety of proteins [2,3].

When measuring thermophoresis over temperature, information about the thermal stability of biomolecules are accessible. We find clear melting transitions and resolve intermediate conformational states. With this it is possible to analyze single nucleotide polymorphisms, DNA modifications and conformational states. The thermophoretic melting analysis is also applicable to proteins where unfolding patterns comparable to scanning calorimetry are found.

[1] Duhr,S & Braun,D Proc. Natl Acad. Sci. USA 103, 19678 (2006).

[2] Baaske,P et al. Angew. Chem. Int. Ed. 49, 2238 (2010).

[3] Wienken,CJ et al. Nat. Commun. 1:100 (2010).