Three persons have been awarded the Nobel prize in chemistry for developing a technique to visualize biomolecule. Jacques Dubochet, Joachim Frank, and Richard Henderson will receive equal shares of the 9m Swedish kronor prize, which was announced by the Royal Swedish Academy of Sciences in Stockholm on Wednesday. Jacques Dubochet, Joachim
Jacques Dubochet, Joachim Frank, and Richard Henderson receive £825,000 prize for their contribution in their field. Dubochet, a Swiss and an honorary professor at the University of Lausanne, pioneered a flash-freezing method that turned the water inside cells into a glassy solid, rather than ice crystals which would damage the cellular structure.
His vitrification technique allowed biological samples to be frozen while retaining their natural shape. Joachim Frank, a German professor at Colombia University in New York, developed mathematical algorithms that allowed the method to be applied to a wider array of molecules. Henderson, a Scottish scientist, and professor at the MRC Laboratory of Molecular Biology was the first to successfully modify the electron microscope to image a protein involved in photosynthesis, by using a weaker beam and taking pictures from many angles.
“This method has moved biochemistry into a new era,” the Royal Swedish Academy of Sciences said in his statement. The technique, called cryo-electron microscopy, allowed biomolecules to be visualized in their natural configuration for the first time, triggering a “revolution in biochemistry”, according to the Nobel committee.
The latest versions of the technology will help the scientists to record biochemical processes as they unfold in film-like sequences. Earlier X-Ray crystallography was used and this technique required samples to be studied in a rigid state, revealing little about the dynamics of proteins and enzymes – many of which could not be successfully crystallized in any case.
Then the electron microscope was introduced that was only suitable for imaging dead matter because its powerful beam destroyed delicate biological structures. Now, this new technique which is Cryo-electron microscopy has allowed scientists to explore the architecture of everything from the proteins that cause antibiotic resistance to the surface of the Zika virus.
Last year the 3D structure of the enzyme producing the amyloid of Alzheimer’s disease was published using this technology. By capturing snapshots of the same system at different time-points, scientists can even stitch together jittery film sequences of biological processes as they unfold. This has paved the way for both new basic insights into life’s chemistry and for the development of pharmaceuticals.
According to Barry Fuller, a surgical sciences’ professor at University College London Medical School says, “The technology is aimed at imaging biomolecules in the life process ‘frozen’ in time – so they are called to an immediate halt”.
Last year’s prize went to three European chemists for developing “nano-machines”, an advance that paved the way for the world’s first smart materials.
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