Prof. dr. Albert J.R. Heck

The research of prof. dr. Albert J.R. 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 post-translational 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. The Heck group has a track record in proteomics and especially in the analysis of protein post-translational modifications. He has 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, for example 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.