The Netherlands Society for Biochemistry and Molecular Biology (NVBMB) each year acknowledges the work of a highly talented young Dutch biochemist or molecular biologist with at least two years of postdoctoral experience. Important criteria include scientific quality, publication in top journals, productivity, creativity, international experience and visibility.
Last year, Simone Lemeer, Utrecht University, was awarded with this NVBMB-prize. As part of the prize she’s invited to organise a NVBMB symposium. She will be your host for the day.
Wednesday, 2 November 2016, 09.00-17.00 Boothzaal, Universiteitsbibliotheek Heidelberglaan 3, De Uithof, Utrecht
Confirmed speakers:
Prof.dr. Bernard Küster Technische Universität München
Prof.dr. Jesper V. Olsen University of Copenhagen
Prof. dr. Petra van Damme VIB, Ugent
Prof.dr. Madelon Maurice University Medical Center Utrecht
Prof.dr. Michiel Vermeulen Radboud Institute for Molecular Life Sciences, Nijmegen
Prof.dr. Jeroen den Hertog Hubrecht Institute, Utrecht
The Royal Netherlands Academy of Arts and Sciences has awarded the 2016 Dr H.P. Heineken Prize for Biochemistry and Biophysics (a sum of USD 200,000) to Jennifer Doudna, Professor of Biomedical Sciences at the University of California in Berkeley (United States).
Jennifer Doudna will receive the Dr H.P. Heineken Prize for Biochemistry and Biophysics for her pioneering research into the structure and functioning of RNA molecules and RNA protein complexes.
On 28 September Jennifer Doudna will give the Heineken Lecture ‘The structural biology and applications of the CRISPR-Cas technology’ at Utrecht University.
Registration
Attendance is free of charge, but we kindly ask you to register. If you didn’t registered yet, please do so here.
The Dutch Society for Mass Spectrometry (NVMS) has honoured Albert Heck with the Outstanding Research Award 2016. Heck received the award for his many excellent contributions to the field of Mass Spectrometry. Heck is Professor of Biomolecular Mass Spectrometry and Proteomics at Utrecht University, and Scientific Director of the Netherlands Proteomics Centre and the large-scale research facility Proteins At Work.
The NVMS was founded in 1964 and is part of the KNCV and NNV. The NVMS welcomes everyone interested in Mass Spectrometry and organizes twice-yearly a national Mass Spectrometry meeting and every two years an international Mass Spectrometry event. Recipient of the 2014 Award is Jeroen Krijgsveld (DKFZ).
Within five years, the first hospitals should be able to completely analyse all of the proteins in a patient’s blood and urine in order to provide more individualised treatment. That is the ambition of the researchers at Utrecht University and their four European partners. The researchers have received a 3.7 million Euro grant for their MSmed research proposal as part of the Future and Emerging Technologies programme within the Horizon 2020 project. On 14 and 15 January, MSmed officially kicked off its activities at an event in Copenhagen.
“Our goal with MSmed is to make large-scale protein analysis faster, cheaper and more complete by a factor of five. If we are successful, then protein analysis can be used at a grand scale in clinical applications”, according to Albert Heck, Professor at Utrecht University and Scientific Director of Proteins at Work. Utrecht University Endowed Professor Alexander Makarov is also involved in the MSmed research programme. Makarov is Director of Global Research for Life Sciences at Thermo Fisher Scientific. The programme coordinator is Prof. Matthias Mann, who holds an honorary doctorate from Utrecht University.
Early and specific diagnosis
The function and interaction of the millions of proteins in our cells determine how we function and feel. Changes to these interactions in our protein metabolism can result in illness, so information about our personal proteome can contribute to early and extremely specific diagnosis and therapies custom-tailored to the individual.
Cooperation by European pioneers
The MSmed programme combines the efforts of five European pioneers in the field of proteomics. The coordinator is Prof. Matthias Mann from the Max Planck Institute for Biochemistry in Martinsried. He and Prof. Jesper Olsen hold appointments at the University of Copenhagen, where they already frequently work together with the doctors from the hospital next door. Prof. Jürgen Cox of the Max Planck Institute for Biochemistry in Martinsried is a specialist in bioinformatics. His expertise is needed to process the millions of measurement data collected. Professors Alexander Makarov and Albert Heck lead the way in the development of new instruments and technologies for faster and more complete analyses.
Proteins at work
The participation in the MSmed research programme is a good fit with Proteins At Work, a national partnership led by Albert Heck that was founded in 2014 to make proteomics accessible to non-specialists who wish to conduct biomedical research. Proteins At Work is funded in part by a grant of 13.5 million Euros from the National Road Map for Large-scale Research Facilities, an initiative by research financier NWO. For more information, see: http://www.netherlandsproteomicscentre.nl/paw
The NPC Progress Meeting 2016, which will be held on 10 February 2016 in the Academiegebouw in Utrecht, puts the spotlight on research of Proteins At Work, a programme of the Netherlands Proteomics Centre, and other developments in the field of proteomics.
Thanks to the work by Utrecht University researcher Fan Liu and her colleagues, it is now possible to map the interactions between proteins in human cells. Until now, this had only been possible when a small number of proteins were brought together in an artificial setting. “We are now able to see which proteins work together and where they are linked”, explains Prof. Albert Heck. “This is essential in order to understand how proteins operate in a cell under healthy conditions, and what goes wrong in diseases.” The results of their research were published in Nature Methods on 28 September.
The millions of proteins in our cells conduct all of the processes that regulate life, in constantly shifting interactions. These interactions are a lively dynamic of links between proteins – often numbering in the hundreds. Until recently, pharmaceuticals inhibited a single protein, but it is more effective to treat diseases by sabotaging the interactions between proteins. This is because the protein inhibited may actually have another useful, or even vital function in a healthy cell, which often results in undesirable side effects during treatment.
Identifying all of the links at a single glance The technique for identifying the cooperation between proteins is called ‘cross-linking mass spectrometry’. This technique has been available for some time, but until now it could only make these interactions visible if a small number of purified proteins were placed together in a small container. However, only a limited amount of information can be derived in such an artificial setting. But now, thanks to improvements in mass spectrometry sequence analysis and a new search algorithm, researchers can study all of the links between all of the proteins present in a cell at a single glance.
From dozens to thousands “We’ve managed to identify around 2,100 of these links, while before we were only able to map out tens or hundreds”, according to Albert Heck, Professor of Biomolecular Mass Spectrometry and Proteomics at Utrecht University. “For example, we have identified more than 100 links in the ribosome, the machine that is responsible for protein synthesis in the cell. Plus, we’ve been able to differentiate between the partners that collaborate with one another all the time from those with more superficial partnerships in this protein complex.”
Publication Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry Fan Liu, Dirk Rijkers, Harm Post and Albert Heck (all from Utrecht University)
Nature Methods, online publication Monday, 28 September, 16:00,doi:10.1038/nmeth.3603
