ESI Q-TOF Mass Spectrometer with UHPLC

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In frame of the biomolecular and biomedical research at the Technical University of Munich (TUM) proteins serve both as research subjects – with regard to biocatalytic or receptor binding activities as well as structural analysis – and as bioactive reagents in cell biology, biomedicine and animal experiments. To this end, highly pure and biochemically precisely characterized protein preparations are needed while electrospray ionization mass spectrometry (ESI-MS) provides final and well documented proof of the molecular composition of the intact protein. ESI-MS offers essential information, both to confirm genetically encoded mutations (either as natural variations or as result of protein engineering) and to identify posttranslational modifications, which may vary depending on the host organism. In this context, proteomics methods are of limited value since peptide-based mass spectrometry just provides infomation about isolated segments of a polypeptide. Insight into the complete composition of a protein or even the homogeneity of a protein preparation (as measured by direct injection without previous chromatographic fractionation) is only available by means of a suitably equipped ESI-MS instrument, which even allows the analysis of complexes between proteins and molecular interaction partners (metal ions, small molecule ligands, nucleic acids, other proteins) under appropriate measurement conditions. Such data are generally required today for publications in renowned scientific journals and are also instrumental as quality control for the application of proteins in animal studies as well as in translational biomedical research. Since a 10 year-old instrument at the life science campus Weihenstephan of TUM will soon face cease of use after the recent expiry of the manufacturer's maintenance, a new ESI Q-TOF mass spectrometer with UHPLC according to the current state of technology is requested. This investment will, on the one hand, provide the future instrumentation basis for internationally competitive research at TUM in protein science, especially in the area protein engineering & design and including its advancement with the cotranslational incorporation of non-natural amno acids; on the other hand, this unique instrument at TUM will boost research in the life sciences at international level, not only at the School of Life Sciences in Weihenstephan as well as other Schools of TUM but also in the frame of multiple collaborations with the Munich University Hospital rechts der Isar (MRI). The professional operation and broad access by users will be guaranteed via affiliation with the Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) at the Campus Weihenstephan.