Heptares founder Richard Henderson receives Nobel Prize in Chemistry 2017

09-Oct-2017

Heptares Therapeutics is delighted that one of its founders, Richard Henderson (MRC Laboratory of Molecular Biology, Cambridge, UK), was awarded the Nobel Prize in Chemistry 2017 together with Jacques Dubochet (University of Lausanne, Switzerland) and Joachim Frank (Columbia University, New York, USA) "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution."

Cryo-electron microscopy (cryo-EM) is a technique for determining three-dimensional information about protein structures at the molecular level. Along with traditional methods for structure determination, such as x-ray crystallography and nuclear magnetic resonance spectroscopy, cryo-EM can reveal the structure of complex molecular assemblies to near atomic level. Detailed information, such as this, is expected to improve understanding of the structure and function of proteins under investigation, and thereby advance the design of new drugs targeting specific proteins. Heptares is applying the techniques of cryo-EM to study G protein-coupled receptor (GPCR) protein complexes, the insights from which are helping to advance the discovery of potential new medicines.

Malcolm Weir, CEO and co-founder Heptares, said: “We are delighted that Richard has received this most prestigious of awards. It is very well deserved and justified recognition of his outstanding contribution to science as a true pioneer of structural biology. His work on membrane protein structure in particular provided the inspiration and scientific foundation for Heptares’ work on GPCR structure-based drug design, and we continue to benefit enormously from his contributions. We would like to offer Richard and his fellow prize winners our warmest congratulations for this fantastic achievement.”

Richard Henderson co-founded Heptares Therapeutics with Malcolm Weir, Fiona Marshall and Chris Tate in 2007.

Heptares Therapeutics Ltd

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Facts, background information, dossiers
  • structural biology
  • protein structure
  • protein complexes
  • molecular biology
  • Nobel Prize for Chemistry
  • cryo-electron microscopy
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