The 2017 Nobel Prize in chemistry has been awarded to three scientists for improving images made of biological molecules.
Jacques Dubochet, Joachim Frank and Richard Henderson will share the nine million kronor (£831,000) prize.
They were named at a press conference in Stockholm, Sweden.
They developed a technique called cryo-electron microscopy (cryo-EM), which simplifies the process for looking at the machinery of life.
The process makes it possible for life’s molecular building blocks to be captured mid-movement and allowed scientists to visualise processes that had never before been seen.
Prof Dubochet was born in Switzerland, Joachim Frank is German and Richard Henderson is from Edinburgh, UK.
Speaking to journalists over a telephone line, Prof Frank said the practical uses for the technique were “immense”.
And the Nobel committee said the work had “moved biochemistry into a new era”.
Committee chair Sara Snogerup Linse explained: “Soon, there are no more secrets, now, we can see the intricate details of the biomolecules in every corner of our cells and every drop of our body fluids.
“We can understand how they are built and how they act and how they work together in large communities. We are facing a revolution in biochemistry.”
Cryo-electron microscopy has been used to capture images of Salmonella’s “injection needle” for attacking cells, proteins involved in antibiotic resistance and the molecular structures governing circadian rhythm – the subject of this year’s medicine and physiology Nobel.
When researchers began to suspect that the Zika virus was behind the microcephaly seen in newborns in Brazil, they turned to cry-EM to visualise the virus. Over a few months, 3-D images of the virus at atomic resolution were generated and researchers could start searching for potential targets for drugs.
Joachim Frank made the microscope technology more easy to apply in a general setting by processing images of the molecules in such a way that fuzzy two-dimensional images were turned into sharp, 3-D structures.
Jacques Dubochet managed to cool water so rapidly that it solidified around a biological sample, allowing its natural shape to be preserved.
Later, Richard Henderson succeeded in presenting the structure of a bacterial molecule at atomic resolution – moving the technique on still further.
He said: “I am delighted for everybody in the field that the Nobel Prize for chemistry has been awarded to acknowledge the success of cryo-EM. I am particularly pleased that Jacques Dubochet has been recognised as the key person who kick-started the field with his method of rapid-freezing in the early 1980s, a crucial advance.”
Dr Henderson was at a scientific meeting when the Nobel Committee tried to contact him: “I was there happily listening to talks… and then the phone rang at about 10:10 – and I rarely get phone calls from Sweden but I’m surrounded by the audience so I rejected the phone call. And then it rang again and I thought I had better (take it) so I went outside and called back,” he explained.
The president of the American Chemical Society (ACS), Allison A Campbell, commented: “This discovery is like the Google Earth for molecules in that it takes us down to the fine detail of atoms within proteins.
“Understanding proteins in their native state is important to every field of science as they are in every living thing. A picture truly is worth a thousand words, and the laureates’ discoveries are invaluable to our understanding of life and the development of new therapeutics.”
The president of the UK’s Royal Society, Venki Ramakrishnan said: “This is revolutionising the way we are able to see how biological molecules look – we can catch them in the act (in chemical reactions), we can see how they work, and so it’s simply changing our understanding of biology.”
Richard Henderson is the 15th Nobel laureate to work at the Medial Research Council (MRC) Laboratory of Molecular Biology in Cambridge.
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Previous winners of the Nobel Prize in Chemistry
2016 – Jean-Pierre Sauvage, Fraser Stoddart and Bernard Feringa shared the prize for the making machines on a molecular scale.
2015 – Discoveries in DNA repair earned Tomas Lindahl and Paul Modrich and Aziz Sancar the award.
2014 – Eric Betzig, Stefan Hell and William Moerner were awarded the prize for improving the resolution of optical microscopes.
2013 – Michael Levitt, Martin Karplus and Arieh Warshel shared the prize, for devising computer simulations of chemical processes.
2012 – Work that revealed how protein receptors pass signals between living cells and the environment won the prize for Robert Lefkowitz and Brian Kobilka.
2011 – Dan Schechtman received the prize for discovering the “impossible” structure of quasicrystals.
2010 – Richard Heck, Ei-ichi Negishi and Akira Suzuki were recognised for developing new ways of linking carbon atoms together.
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