Dr. Michael Mormann
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mmormann@uni-muenster.de http://www.campus.uni-muenster.de/hyg_forsch_dreisewerd.html |
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Structural characterization of proteins and glycoconjugates represents a prerequisite for understanding for their interplay in non-covalent interaction. Mass spectrometry (MS) is considered as a key technology for the elucidation of molecular structures of interacting biomolecules. The group has developed and implemented novel matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF), electrospray ionization quadrupole time-of-flight (ESI-QTOF) and high field Fourier-transform ion cyclotron resonance (FT-ICR) MS methodologies and new MS fragmentation protocols for de-novo sequencing to proteomics and glycomics to achieve high confidence structural and heterogeneity analysis. High resolution FT-ICR mass analyzers provide unique specifications such as high sensitivity, high mass accuracy as well as high resolving power giving rise to fast and very often unambiguous characterization of biopolymers. However, when complex mixtures from biological matrices are considered for analysis analytical strategies often are comprised of a combination of separation techniques, e.g., 1- and 2-D gel electrophoresis, liquid chromatography (LC), thin-layer chromatography (TLC) or capillary electrophoresis (CE) and mass spectrometry.
The group carried out a number of research projects in cooperation with German, European and Indian university groups. The group is collaborating on specific topics and technologies with industrial labs in a bilateral way. We are working strongly interdisciplinary within an international network of (bio-)chemists, physicists, biologists, biotechnologists and clinicians.
