Nobel Prize In Chemistry Awarded For Method That Help Visualise Biomolecules


Stockholm: The 2017 Nobel Prize in Chemistry was awarded to France’s Jacques Dubochet, Britain’s Richard Henderson and the US scientist Joachim Frank, for the development of a method called Cryo-electron microscopy. This can help detect and visualise complex biomolecule structures.

This technique of studying molecules has ensured great applications in field of biochemistry, according to the Nobel Committee. The 9-million-kronor ($1.1 million) prize is shared by Dubochet of the University of Lausanne, Frank at New York’s Columbia University and Henderson of MRC Laboratory of Molecular Biology in Cambridge, Britain.

Cryo-electron microscopy gives scientists the opportunity to look at the machinery of life in 3D form. This was something that was not possible with earlier forms of electron microscopes as more powerful beams would destroy the biological matter.

The specific type of electron microscopy is based on the principle of forming a three-dimensional image by collecting and combining thousands of projections of the biomolecules. Specimens that are to be analysed remain in their native state without the need for dyes or fixatives. This allows the study of fine cellular structures, viruses and protein complexes at molecular resolution.

In the announcement ceremony held at the Royal Swedish Academy of Sciences, the committee explained how the technique allows researchers to “freeze biomolecules mid-movement and visualize processes they have never previously seen.” The development, they said, “is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.”

According to the committee’s statement, Richard Henderson in 1990 was successful in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. Joachim Frank made the technology more widely applicable. Jacques Dubochet helped with vitrification of water, which ensured that the biological sample retained its natural shape even in the vacuum and while frozen.

As the committee notes, the work produced by these three scientists has ensured that now researchers have access to 3D structures of biomolecules. This includes proteins which cause antibiotic resistance to seeing the surface of the Zika virus in full detail.