Research
Focus
Structural mass spectrometry
method development
- novel covalent labeling and cross-linking chemistry of proteins /nucleic acids
- new acid proteases as a tool for protein digestion
- automation of HDX-MS and CX-MS workflow including software design
Functionalized surfaces for mass spectrometry
- ambient ion landing protein immobilization
- surface Immuno-affinity substrates for clinical diagnostics
- biochemically active plates for desorption mass spectrometry
Projects
- European Proteomics Infrastructure Consortium providing access
- European Network of Fourier-Transform Ion-Cyclotron-Resonance Mass Spectrometry Centers
- Mapping the protein surface accessible area utilizing Top Down mass spectrometry and reactive radical footprinting.
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European Network of Fourier-Transform Ion-Cyclotron-Resonance Mass Spectrometry Centers
The European Proteomics Infrastructure Consortium providing access (EPIC-XS) consists of a unified network of experienced access providers and research groups who share a common goal; to facilitate the development and sustainability of proteomics exploration to all life science researchers within the European Union. The initiative is coordinated by Albert Heck, professor of Biomolecular Mass Spectrometry and Proteomics at Utrecht University. EPIC-XS will provide scientists transnational access to high end proteomics technologies and resources. The project will strengthen and expand the European proteomics community through its expertise in proteomics. It’s excellent training courses and programs, available to both novices and experts, will attract new research communities who will be schooled in advanced proteomics technologies. The initiative brings together some of the most world renowned proteomics laboratories and researchers. The community has expertise in accommodating and guiding researchers within the life sciences, as many of the members also participated in the pan- European PRIME-XS initiative, which ended in 2015.
Funded by EU H2020 (EPIC-XS)
European Network of Fourier-Transform Ion-Cyclotron-Resonance Mass Spectrometry Centers
EU_FT-ICR_MS proposal aims to establish a European network of FT-ICR (Fourier Transform Ion Cyclotron Resonance) mass spectrometry (MS) centers in association with a manufacturer and a SME software company. Mass spectrometry (MS) has become the most ubiquitous analytical techniques in use today, providing more information on the composition and the structure of a substance from a smaller amount of sample than any other techniques. Unlike other analytical techniques, such as NMR, which mainly rely on a unique technology, MS is characterized by the existence of a large range of mass analyzers. FT-ICR MS is the most powerful MS technique. It offers up to 100 fold higher mass resolving power and mass accuracy than any other MS technique. On the contrary to NMR community with which the FT-ICR MS shares several features, FT-ICR MS has never been involved in a European INFRA network and so will be a legitimate candidate to the Integrating Activities for Starting Communities call. The EU_FT-ICR_MS network includes 10 FT-ICR MS centers from 8 different European countries (Belgium, Czech Republic, Finland, France, Germany, Italy, Portugal, and United Kingdom) and 1 third country (Russia), a European FT-ICR MS manufacturer and 2 SMEs. It includes centers equipped with up-to-date FT-ICR MS and expertise which will cover most of the field in which FT-ICR mass spectrometry is involved: BioOrganic & BioInorganic, Cultural heritage, Glycomics, Environment, Imaging, InfraRed Spectroscopy of Ions in the Gas Phase, Lipidomics, Medicine, Petroleum & Coal Oil, Nanoparticles, Organic chemistry, Physical chemistry, Proteomics, Structural biology. The EU_FT-ICR_MS proposal contains six work-packages which cover all the aspects of the INFRAIA-02-2017 (RIA) Integrating Activities for Starting Communities (WP1 Transnational access; WP2 Training and Education; WP3 Open Data and e-Infrastructure; WP 4 Joint Research Action; WP 5 Dissemination; WP6 Consortium management).
Funded by EU H2020 (EU_FT-ICR_MS)
Mapping the protein surface accessible area utilizing Top Down mass spectrometry and reactive radical footprinting.
Structural proteomics has become an emerging technique of current structural biology. It covers very broad range of analytical methods from hydrogen/deuterium exchange to chemical crosslinking. Although, the limitations and potentials of both techniques are well studied, foundations of covalent labelling are still poorly described. While H/D exchange offers information about backbone accessibility, covalent labelling targets amino acid side chains and thus provides complementary structural information. In this proposal we will develop chemical reagents with novel reactivity that will allow targeting of more amino acid side chains and expand the spatial resolution of the method. We will also pursue hydroxyradical footprinting where we aim mainly at the development of top-down mass spectrometric approaches allowing to assign not only the site of the modification but also to assess the reactivity scale of individual modified residues. Such advancements will greatly facilitate protein structure characterization and will provide valuable information for protein structure modelling.
Funded by Czech Science Foundation (19-16084S)