Research Group HECK

Biomolecular Mass Spectrometry and Proteomics group, Departments of Chemistry and Pharmaceutical Sciences
Contact: Prof. Albert J. R. Heck
E-mail: A.J.R.Heck@uu.nl
Website: http://bioms.chem.uu.nl/index.php/groupp-members/people/userprofile/heck

General research focus: Proteomics and biomolecular mass spectrometry technologies

The Biomolecular Mass Spectrometry and Proteomics group is organizationally embedded in the Bijvoet Research Institute and the Utrecht Institute for Pharmaceutical Sciences, both research schools at Utrecht University. The Heck group houses on of the largest research infrastructures for mass spectrometry based proteomics and structural biology, the two pillars of our research program.

The Heck laboratory has a track record in proteomics and especially in the analysis of protein post-translational modifications. We introduced TiO2 as enrichment material for the targeted analysis of phosphopeptides, and implemented this technique into a miniaturized on-line automatic system, and on a micro-chip device. We introduced the use of a protease named LysN, that in conjunction with ETD provides unique sequence ladders, that are straightforward to interpret and allow facile de novo sequencing and improve the analysis of protein phosphorylation. We also have an extensive track-record in quantitative proteomics, introducing metabolic stable isotope labeling in multicellular organisms such as Drosophila and C. elegans, using SILAC for studying stem cell and B cell differentiation, and stable isotope labeling by using chemical approaches. The latter method we most recently also implemented to follow differential pTyr phosphorylation in differentiating stem cells. Bioinformatics support and expertise to provide state-of-the-art data, pathway and network analysis is available.

The Heck laboratory is also a pioneer in macromolecular or native mass spectrometry, which enable the analysis of intact protein assemblies by mass spectrometry. The Heck group develops mass spectrometers dedicated for this work and applies these technologies to study the structure and dynamics of for instance transcription complexes, bacteriophages and virus assembly.

Back