Fourier Transform Mass Spectrometer
Project management at the University of Würzburg:
The specificity, thermodynamics and kinetics of protein-protein interactions are determining factors for signal transduction at bilolgical membranes and this for the control of behaviour, differentiation and development of cells. In this project, high resolution mass spectrometry with am mass range up to 100 kDa (ESI-FT-ICR-MS) will be used to clarify important aspects of recognition mechanisms of reulatory membrane proteins.
It is planned to produce recombinant receptor domains, protein ligands and signal proteins, in order to examine the interactions between them, qualitativly and quantitativly. In particular, it is to be orobed (1) which requirements (affinities, residues of contract) must be met for demonstration of noncovalent complexes by mass spectrometry, (2) to what extent mutant proteins with changes binding properties can be identified, and (3) whether conformational changes of protein during formation of complexes can be demonstrated througt differences in ionizabilities.
A second major project is to investigate how far refolding of recombinant proteins (renaturation) can be followed by MS measurements. For this purpose, C13- and N15- depleted proteins shall be produced and employed.
The mass spectrometry project will be closely linked, scientifically as well as concerning staff, with the recently evaluated SFB 1756 ("Regulatory membrane proteins. From recognition mechanism to pharmacologic target structure").
Projekt period: from 01.2000 to 12.2012
DFG ,Granting date: 25.10.1999