Nobel Prize: Mapping Moving Biomolecules

What won the 2017 Nobel Prize for Chemistry?
10 October 2017

Interview with 

Tony Crowther, Laboratory of Molecular Biology


Imaging Biomolecular movement


Next on our Nobel Prize list is Chemistry, which was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson for their work on an imaging technique called cryo-electron microscopy. Tony Crowther uses electron microscopy in his research and has known Richard for many years as a colleague at the Laboratory of Molecular Biology in Cambridge. And many thanks to MRC for providing us with audio from the winner himself, Richard Henderson...

Richard - I’m delighted to be sharing the Nobel Prize. I think…

Tony - To understand the way life works in health and disease, it’s necessary to know the detailed structures of the complex molecules involved. Many processes in the cells of all living things depend on large, dynamic, molecular machines. Previously this required making crystals of the molecule and solving the atomic structure by X ray crystallography. This could be difficult as important molecules or complexes might not crystallise and movements in the molecules key to their function would be inaccessible.

This has all changed with recent developments in cryo-electron microscopy, particularly in electron microscopes, in electron detectors, and in computer software. The molecule of interest can be trapped in a frozen state and its atomic structure determined by computer averaging of multiple images of views in different directions. This may also illuminate different conformations important in understanding the function of a molecule.

The newly developed technique, still open to some improvements, will be useful to all biologists interested in molecular structures and to pharmaceutical companies involved in drug development. For example, already in the LMB the structure of the tau protein filament important in Alzheimer’s disease has recently been solved.

Richard - So we think in a few years, or five years we might know most of the structures certainly in the human biological population and then in pathogenic bacteria. So really it’s quite an exciting time.


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