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Jacques Dubochet, Joachim Frank, Richard Henderson Get Nobel Prize in Chemistry
05 October 2017, 12:19 | Todd Saunders
Martin Luther King woken up by Stockholm's Lucia in 1964
Joachim Frank, PhD, a professor of biochemistry and molecular biophysics and of biological sciences at Columbia, shares the award with Richard Henderson, of Cambridge University in Britain, and Jacques Dubochet, a professor at the University of Lausanne in Switzerland.
Dubochet, Frank and Henderson developed a method that made it possible to see the molecules of life for the first time as three-dimensional structures at atomic resolution.
Their research is "decisive for both the basic understanding of life's chemistry and for the development of pharmaceuticals", according to the academy. Pictures were taken from many different angles of the same membrane under the electron microscope to produce a rough 3D model of bacteriorhodopsin's structure.
Henderson was the first one to use an electron microscope to generate a 3D image of a protein at atomic resolution in 1990, showing that the technique could be used on biomolecules and not just dead matter. Using this technique, researchers have been able to study the structure of a variety of biological molecules, from proteins involved in circadian rhythms to the Zika virus.
Cryo-electron microscopy gets around two major challenges when studying large biological molecules with a transmission electron microscope.
Henderson, a professor at the Molecular Research Council (MRC) Laboratory of Molecular Biology in the United Kingdom, produced the first high-resolution model of a protein, bacteriorhodopsin, using electron cryo-microscopy (cryo-EM) in 1990.
USA -based Thermo Fisher Scientific is a leading supplier of cryo-electron microscopy instruments.
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The new approach fills a previously blank space by generating images of everything from the surface of the Zika virus to proteins that cause antibiotic resistance or are involved in Alzheimer's.
This year's Nobel Prize in Chemistry has been awarded to three researchers for their work on a groundbreaking method for imaging complex molecules.
He explained that cryo-electron microscopy emerged back in the 1980s, and has been actively developing over the recent years due to the improvement in tool and computing platforms, including supercomputers. But Hansson pointed out that scientists at the LMB, which offers the same kind of freedom, have won an extraordinary 15 Nobel Prizes. By calling on thermodynamics, biology, computer science, the collective work of Henderson, Frank, Dubochet and others turned cryo-electron microscopy into a pillar of modern biochemistry.
"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.
"Knowing this structure opens up the possibility of rational drug design in this area", Hardy said.
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