"Mass spectrometry enables the characterization of molecules that are present in cells and allows thereby the identification and characterization of proteins and other biomolecules that work together and are involved in cellular processes and in disease."

Albert Heck (b. 1964) is Professor of Chemistry and Pharmaceutical Sciences at Utrecht University and scientific director of the Netherlands Proteomics Center. Heck is a leading expert in protein mass spectrometry. His group develops and implements innovative mass spectrometric methods for the more efficient and detailed characterization of proteins in relation to their biological function. In short, Heck applies protein mass spectrometry to problems in proteomics, glycoproteomics and in structural biology.



Albert Heck received multiple awards, such as the KNCV Golden Medal (2001), the Descartes Huygens Award de la Republique Francaise (2007), NGI Distinguished Visiting Scientist (2010-2011), the Life Science Award of the German Mass Spectrometry Society (2010), the HUPO Discovery Award in Proteomic Sciences (2013), the EuPA Pioneer in Proteomics Award (2014) and the American Chemical Society ‘Frank H. Field and Joe L. Franklin Award for Outstanding Achievements in Mass Spectrometry’ (2015).

In 2017, Albert Heck has been awarded with the Spinoza Award, the most important award in the field of Science in the Netherlands. In 2018 Heck received the Sir Hans Krebs Medal, for his achievements in biochemistry from the Federation of European Biochemical Societies (FEBS) and the J.J. Thomson Medal of the International Mass Spectrometry Society.

Research: mass spectrometric methods for proteins in biological function

The research of Heck focuses on the development and implementation of innovative mass spectrometric methods for the more efficient and detailed characterization of proteins in relation to their biological function. The emphasis is on the structural characterization of proteins and posttranslational modifications as well as the investigation of protein complexes and protein interactions important in e.g. protein folding, protein ligand binding, and the formation of tertiary and quaternary structures. In short we apply protein mass spectrometry to problem in proteomics and in structural biology. As scientific director, myself and my group play a pivotal role in the Netherlands Proteomics Centre, which focuses on developing proteomics technologies, focused on protein expression quantification, membrane protein proteomics, post-translational modifications, protein networks, highthroughput protein analysis and biomarkers.

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.

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 evelops mass spectrometers dedicated for this work and applies these technologies to study the structure and dynamics of for instance transcription complexes and virus assembly.


Biomolecular Mass Spectrometry and Proteomics
Inaugural lecture date