Contact

Professor Hartmut Oschkinat

phone +49 30 94793 160
oschkinat(at)fmp-berlin.de

Department of NMR-Supported Structural Biology
(Hartmut Oschkinat)

 

The main focus of our group is the development of solid-state magic-angle spinning (MAS) NMR methodology as a routine tool for biological studies, in particular for structural characterisation of protein-protein interactions that are responsible for the reception and transduction of signals. This research focuses traditionally on membrane integrated proteins and receptor-ligand complexes.

In recent years a new method for signal enhancement called dynamic nuclear polarisation (DNP) was established and its value tested in structure determination and metabolomic projects. Using DNP, the nascent peptide chain in the tunnel of the ribosome was investigated, and the nature of black deposits in cartilage of Alkaptonuria patients, who suffer from impaired tyrosine degradation. Recently, we started a set of new projects on membrane proteins and inositol lipids in their actual membranes, and on live biofilms. Furthermore, we have started a project on the principles underlying liquid-liquid phase separation, with the protein FUS as an example. Our aim is to provide quantitative information as to individual interactions, responsible for establishing the dense phase and the structural characterization of such interactions. Furthermore, we are investigating proton flows and proton dynamics to understand protein function, funded by the SFB 1078.

 

Protein Expression and NMR Sample Preparation

Staff scientist: Dr. Anne Diehl
 

NMR Facility

Solid-state NMR facility managers: Dr. Matthias Hiller / Dr. Veniamin Chevelkov

Solution-state NMR: Dr. Peter Schmieder

 

 

Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Germany
+4930 94793 - 100 
+4930 94793 - 109 (Fax)
info(at)fmp-berlin.de

Diese Website verwendet Cookies zur Verbesserung des inhaltlichen Angebots. Datenschutz OK