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Mass Spectrometry & Protein Chemistry

Mass spectrometry (MS) has emerged as a core analytical technique in protein chemistry. Driven by the rapid development of instrumentation, analysis methods and  computing tools, MS based proteomics is at the forefront of techniques in modern life sciene research.  The power of modern MS can be illustrated when seen in historic perspective. Sequencing of a single decapeptide by traditional Edman degradation took approximately 10 hours, MS based proteomics can now not only identify several thousands of peptides and hundreds of proteins, but can also collect quantitative information as well as information about posttranslational modifications in the same time at 100 times the sensitivity.

In the Mechtler lab, we are interested in developing new methods to increase sensitivity, accuracy and precision of protein identification/quantification and the detection of post translational modifications, respectively. Our aim is to use these optimized methods to answer fundamental biological processes.

Computational proteomics

Current MS instruments produce vast amounts of data. Therefore, automated data processing pipelines are required. Development in our bioinformatics team currently focuses on

  • improving sensitivity of peptide identification
  • identification and localization of post translational modifications
  • peptide and protein quantification
  • reliable detection of protein interactions
  • quality control

Cross-linking MS

Chemical cross-linking in combination with mass spectrometry (XL-MS) is being increasingly used in proteomics research to gain structural information on proteins and protein complexes. In a cross-linking experiment, a reagent forms covalent bonds between specific residues that are in close spatial proximity to each other, thus revealing distance restraints between residues and hence interaction sites either within a protein or between different proteins. XL-MS has the unique ability to capture dynamic situations in a protein complex, which renders it appropriate to study a range of situations where x-ray crystallography is not applicable. In addition, XL-MS is a very sensitive technique that can be applied to endogenous levels of proteins, and proteins within complex mixtures.

Karl Mechtler

Contact

Karl Mechtler

+43-1-79044 - 4280