Dubochet, Frank & Henderson win Nobel Prize for Chemistry 2017

Allan Goodman
October 6, 2017

Jacques Dubochet, Joachim Frank, and Richard Henderson were jointly awarded the prize by the Royal Swedish Academy of Sciences.

This is Jacques Dubochet, Switzerland, Joachim Frank, of the United States, and Richard Henderson, of the United Kingdom. Dubochet, a biophysicist at the University of Lausanne in Switzerland, advanced electron microscopy toward cryo-EM in the 1980s, when he applied a vitrification technique to samples, allowing them to be rapidly frozen in a way that would not allow water to disturb the electron beams used to create the images.

Jacques Dubochet, Joachim Frank, and Richard Henderson were announced the winners by the Royal Swedish Academy of Sciences in Stockholm. They each take home a share of the SEK 9 million (EUR 945 000) award for their work with cryo-electron microscopy.

"We are facing a revolution in biochemistry", said Nobel Committee Chairman Sara Snogerup Linseduring the announcement, according to CNN. "Cryo-electron microscopy is about to completely transform structural biology", he said.

Being able to capture images of these biological molecules at atomic resolution not only helps scientists to understand their structures, but has opened up the possibility of exploring biological processes by stitching together images taken at different points in time.

"By solving more and more structures at the atomic level we can answer biological questions, such as how drugs get into cells, that were simply unanswerable a few years ago", said Jim Smith, director of science at Britain's Wellcome Trust.

The chemistry prize was the third Nobel announced this week.

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The medicine prize went to three Americans studying circadian rhythms: Jeffrey C Hall, Michael Rosbash and Michael W Young.

In the Zika virus, for example, scientists identified unique parts of the pathogen's structure using cryo-electron microscopy, identifying a potential target for a vaccine. That demonstration of what cryo-EM could achieve was "decisive for both the basic understanding of life's chemistry and for the development of pharmaceuticals", the committee said. In 1990, after more than 15 years of effort, he became the first to use it to produce a picture of a protein, bacteriorhodopsin, that was as detailed as those X-ray crystallography can provide. This was previously thought to be impossible, as the electron beam destroys the biological material. Second, electron microscopes can't be used on anything that's in water, since the process evaporates that water.

It is these three breakthroughs that have led to the technology we have today.

Frank's work between 1975 and 1986 proved that electron microscopes could be applied in general use.

"To give one example, a year ago the 3D structure of the enzyme producing the amyloid (protein) of Alzheimer's disease was published using this technology", Hardy said.

The Nobel prizes are named after the Swedish engineer Alfred Nobel.

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