A Columbia University professor is one winner of the Nobel Prize in chemistry for his work on innovative and better ways to capture images of biomolecules.
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.
“This is an extraordinary day for me,” Frank said at a Columbia news conference on Wednesday. “It’s a very touching, humbling experience, because I know that so many new things are discovered all the time that it’s sort of, the odds are very long to get me to this place.”
Frank, 77, was born in Germany and joined Columbia University in 2008. Though much of this work was done before then, he said joining Columbia was instrumental to meeting colleagues across departments and working with brilliant students who contributed pieces to this “immense puzzle.”
The three were honored for developing “cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution,” by the Nobel Foundation.
What does that mean, exactly? Well, to reach scientific breakthroughs, we must understand our world, including objects at the atomic level that are invisible to the human eye.
It’s been difficult to capture life’s “molecular machinery,” however, meaning we don’t really know what the 3-D structure of biomolecules looks like, which hampers our ability to understand them.
“Cryo-electron microscopy changes all of this,” the Nobel Foundation wrote. “Researchers can now freeze biomolecules mid-movement and visualize processes they have never previously seen, which is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.”
The scientists built on each other’s achievements to reach that goal, and it began with Frank who, between 1975 and 1986, developed an image processing method that analyzed and merged an electron microscope’s two-dimensional images into a clear three-dimensional structure.
In the 1980s, Dubochet was able to cool water so quickly that it solidified without forming ice crystals, instead forming around a biological sample so the biomolecules retained their shape, getting a “freeze frame” of the action.
In 1990, Henderson used an electron microscope to create a 3-D image of a protein at atomic resolution, a breakthrough because previously electron microscopes were thought to only be able to capture images of dead matter, since the electron beam was so strong it would have destroyed biological material.
With these three discoveries, “the electron microscope’s every nut and bolt have been optimised,” according to the Nobel Foundation, but it’s also the application of this technology that is important. By being able to see the 3-D structure of, say, a ribosome – a minute structure within a cell that contained RNA – scientists can learn how ribosomes work in something like the Zika virus. That understanding leads to treatment developments.