MRC Laboratory of Molecular Biology Alumni Awarded Nobel Prize for Chemistry
News Oct 14, 2013
This latest accolade takes the total number of Nobel Prizes awarded for work undertaken at the much-lauded Laboratory of Molecular Biology to 10 and the total number of prizes awarded to MRC-funded scientists to 21 in its 100 year history.
A key part of the Nobel Prize-winning research was undertaken at the MRC Laboratory of Molecular Biology (LMB), in the Structural Studies Division, in the 1970s. Together the work of all three LMB alumni has been developed further and enables modern chemists to simulate complex chemical reactions on a computer. This ability has allowed for much deeper understanding of how chemical processes happen.
Michael Levitt came to LMB as a PhD student in 1968, having first met Arieh Warshel while working as a visitor at the Weizmann Institute, Israel. At the Weizmann, Michael had become interested in protein conformation analysis and had written a general computer programme for studying the conformations of small molecules. He realised that the same programme could form the basis of a system for studying larger molecules. It was this system that Michael developed at LMB during his PhD work.
Martin Karplus, who had a research group in Harvard, was a visitor to LMB from1969 to 1970. He and Arieh worked together at Harvard in the early 1970s; Arieh combined his work with Michael on the classical computer program with Martin’s work on quantum physics. In 1972 Martin and Arieh published a paper showing for the first time how to combine classical and quantum physics when modelling retinal, a molecule embedded in the retina of the eye.
After undertaking post-doctoral work at the Weizmann, Michael returned to the LMB in 1974 and was joined by Arieh. During this time the final obstacles were overcome and two important papers were published in 1975 and 1976. The 1976 paper was the first computerised model of an enzymatic reaction, and for the first time allowed any kind of chemical reaction to be simulated involving any kind of molecule, irrespective of size.
Michael recently reflected on lessons learned during his time at the LMB and working with director Professor Max Perutz in a chapter for the book Memories and Consequences: Visiting Scientists at the MRC Laboratory of Molecular Biology, Cambridge. He wrote:
“In compiling these lessons, it became clear that Max Perutz had influenced me more than anyone else. I have published papers with Max, Francis [Crick] and Aaron [Klug], worked most closely with Aaron Klug and spent two years as Francis Crick’s only postdoctoral fellow shortly after he moved to the Salk Institute in 1977. Max Perutz’s influence on me has been like a fine wine, a little strange at first but maturing over 50 years to be a guiding light to me and, I imagine, to countless others.”
Professor Richard Henderson, former Director at the MRC Laboratory of Molecular Biology and former head of the Structural Studies Division, commented:
“Their early work on energy minimisation and its evolution into molecular dynamics has developed into a world-wide industry. It has permeated into all aspects of structural biology, from protein folding to drug design, to supramolecular interactions. Hopefully, it will soon be possible to compute the structure of almost everything, even if not with perfect accuracy.”
Chinese researchers have developed interfacially polymerized porous polymer particles for low- abundance glycopeptide separation. These polymer particles - with hydrophilic-hydrophobic heterostructured nanopores - can separate low-abundance glycopeptides from complex biological samples with high-abundance background molecules efficiently.