Albert J.R. Heck
|Albert J.R. Heck|
November 25, 1964 |
Goes, The Netherlands
|Occupation||Professor of Biomolecular Mass Spectrometry|
|Known for||Proteomics, Native Mass Spectrometry|
Albert J.R. Heck (born November 25, 1964, in Goes, Netherlands) is a Dutch scientist and professor at Utrecht University, the Netherlands in the field of mass spectrometry and proteomics. He was awarded the Spinoza Prize in 2017.
Albert Heck studied chemistry at the VU University in Amsterdam and received his Ph.D. in 1993 at the University of Amsterdam. After a postdoctoral period at Stanford University in the lab of Richard Zare and Sandia National Laboratories (Livermore) he became a postdoctoral fellow and later lecturer at University of Warwick. In 1998 he accepted a chair at Utrecht University as head of the Biomolecular Mass Spectrometry and Proteomics Group. His group is part of the Departments of Chemistry and Pharmaceutical Sciences of the Faculty of Science. Since 2003 Heck is scientific director of the Netherlands Proteomics Centre. From 2006 until 2012 Heck was scientific director of the Bijvoet Center for Biomolecular Research at the Utrecht University. He is a council member of HUPO Proteomics Standards Initiative (PSI) and since 2011 coordinator of PRIME-XS, a European collaboration in the field of proteomics. In 2013, Heck received the Discovery Award in Proteomic Sciences from HUPO and since 2014 he is a member of the European Molecular Biology Organization. In 2014, Heck was elected a member of the Royal Netherlands Academy of Arts and Sciences.
The research of Albert Heck is focussed on the use of mass spectrometry to study proteins. Within his research group, the two main lines of research are proteomics and native mass spectrometry of proteins and protein complexes. In proteomics, he is most renowned for his work on the analysis of post-translational modification of proteins using mass spectrometry, mainly protein phosphorylation and for the development of novel peptide fragmentation strategies to elucidate site specific post-translational modifications.
His group is among the pioneers of native mass spectrometry to study large protein assemblies and has developed and implemented novel technologies to study protein interactions and the formation of tertiary and quaternary protein structures. Among the complexes that he studied using native mass spectrometry are virus assemblies of up to 18 megadalton  and antibodies in complex with other proteins such as their antigens or the complement system.
Awards and Prizes
- Spinoza Prize (2017)
- The American Chemical Society ‘Frank H. Field and Joe L. Franklin Award for Outstanding Achievements in Mass Spectrometry (2015)
- The UePA Pioneer Proteomics Award (2014)
- The HUPO Discovery Award in Proteomics Sciences (2013)
- Life Science Award of the German Mass Spectrometry Society (2010)
- NGI Distinguished Visiting Scientist (2010-2011)
- Descartes Huygens Award of the Republique France (2007)
- The KNCV golden medal (2001)
- "Hoogleraren" (in Dutch). Volkskrant. September 5, 2012. Retrieved 2014-05-21.
- "Eight million euros for European Network led by Albert Heck". Netherlands Genomics Initiative. March 4, 2011. Retrieved 2012-03-20.
- "Most important international proteomics award for Albert Heck". Netherlands Genomics Initiative. October 2, 2013. Retrieved 2014-05-21.
- "EMBO announces new members for 2013". EMBO. May 21, 2014. Retrieved 2014-05-21.
- "Albert Heck en Ineke Braakman verkozen tot EMBO leden" (in Dutch). Utrecht University. May 19, 2014. Retrieved 2014-05-21.
- "KNAW kiest zeventien nieuwe leden" (in Dutch). KNAW. May 21, 2014. Retrieved 2014-05-21.
- "Moeilijk te vangen fosforgroepen" (in Dutch). Chemisch2Weekblad (C2W) Life Sciences. June 23, 2012.
- "Interview - Albert Heck". SharedProteomics. Retrieved 2014-05-21.
- "Awards - 2013 Recipients". HUPO. Retrieved 2014-05-21.
- "Grote complexen intact de MS in" (in Dutch). Chemisch2Weekblad (C2W). June 7, 2013.
- "Een moleculaire rattenkoning slaat groot immuunalarm" (in Dutch). NRC Handelsblad. March 15, 2014.