Richard Henderson (biologist)

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Richard Henderson
FRS FMedSci
Born (1945-07-19) 19 July 1945 (age 78)
Edinburgh, Scotland
EducationUniversity of Edinburgh (BS)
University of Cambridge (PhD)
Known forSingle-particle cryo-electron microscopy
AwardsNobel Prize in Chemistry (2017)
Scientific career
FieldsStructural biology
Cryo-electron microscopy
InstitutionsLaboratory of Molecular Biology
Doctoral advisorDavid Blow

Richard Henderson FRS FMedSci (born 19 July 1945)[1] is a Scottish molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. He shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank.

Career

Henderson worked on the structure and mechanism of chymotrypsin for his Ph.D. with David Blow at the MRC Laboratory of Molecular Biology.[2] This interest in membrane proteins led to him working on voltage-gated sodium channels as a post-doctoral researcher at Yale University. Returning to the MRC Laboratory of Molecular Biology in 1975, Henderson worked with Nigel Unwin to study the structure of the membrane protein bacteriorhodopsin by electron microscopy. A seminal paper in Nature by Henderson and Unwin (1975)[3] established a low resolution structural model for bacteriorhodopsin showing the protein to consist of seven transmembrane helices. This paper was important for a number of reasons, not the least of which was that it showed that membrane proteins had well defined structures and that transmembrane alpha-helices could occur. After 1975 Henderson continued to work on the structure of bacteriorhodopsin without Unwin. In 1990 Henderson published an atomic model of bacteriorhodopsin by electron crystallography in the Journal of Molecular Biology.[4] This model was the second ever atomic model of a membrane protein. The techniques Henderson developed for electron crystallography are still in use.

Together with Chris Tate, Henderson helped develop conformational thermostabilisation: a method that allows any protein to be made more stable while still holding a chosen conformation of interest.[5][failed verification] This method has been critical in crystallising and solving the structures of several G protein–coupled receptors (GPCRs).[6] With help from the charity LifeArc, Henderson and Tate founded the MRC start-up company, Heptares Therapeutics Ltd (HTL) in 2007.[7] HTL continues to develop new drugs targeting medically important GPCRs linked to a wide range of human diseases.[8] [9]

In the last few years, Henderson has returned to hands-on research focusing on single particle electron microscopy. Having been an early proponent of the idea that single particle electron miscroscopy is capable of determining atomic resolution models for proteins, explained in a 1995 paper in Quarterly Reviews of Biophysics,[10] Henderson aims to be able to routinely obtain atomic structures without crystals.[11] He has made seminal contributions to many of the approaches used in single particle electron miscroscopy, including pioneering the development of direct electron detectors that recently allowed single particle cryo-electron miscroscopy to achieve this goal.

Although Henderson has typically worked independently, he has trained a number of scientists who have gone on to independent research careers. These scientists include:

Life

Henderson was educated at Boroughmuir High School and Edinburgh University (B.Sc. Hons in Physics, 1st Class). He completed his PhD research under the supervision of David Blow at the Medical Research Council Laboratory of Molecular Biology and received the degree from Cambridge University in 1969. He has worked at the Medical Research Council's Laboratory of Molecular Biology (MRC LMB) in Cambridge since 1973, and was its director between 1996 and 2006.[12] He was also a visiting professor at the Miller Institute of the University of California, Berkeley in Spring 1993.[13] He is currently a mentor for the Academy of Medical Sciences Mentoring Scheme.[14] Outside academia, he lists his interests as hill walking in Scotland, kayaking and drinking good wine.[15]

Awards[12]

References

  1. ^ HENDERSON, Dr Richard, Who's Who 2014, A & C Black,2014; online edn, Oxford University Press, 2014
  2. ^ Dr Richard Henderson FRS FMedSci Fellow Profile,Academy of Medical Sciences
  3. ^ "Three-Dimensional Model of Purple Membrane Obtained by Electron Microscopy". Nature. 257: 28–32. doi:10.1038/257028a0.
  4. ^ Henderson, R; Baldwin, JM; Ceska, TA; Zemlin, F; Beckmann, E; Downing, KH. "Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy". Journal of Molecular Biology. 213: 899–929. doi:10.1016/S0022-2836(05)80271-2. PMID 2359127.
  5. ^ http://www2.mrc-lmb.cam.ac.uk/group-leaders/t-to-z/chris-tate/
  6. ^ Warne, T; Serrano-Vega, MJ; Baker, JG; Moukhametzianov, R; Edwards, PC; Henderson, R; Leslie, AG; Tate, CG; Schertler, GF (24 July 2008). "Structure of a beta1-adrenergic G-protein-coupled receptor". Nature. 454 (7203): 486–91. doi:10.1038/nature07101. PMID 18594507.
  7. ^ https://www.heptares.com/
  8. ^ https://www.heptares.com/company/
  9. ^ Dr Richard Henderson FRS FMedSci Fellow Profile,Academy of Medical Sciences
  10. ^ Henderson, R (February 2004). "Realizing the potential of electron cryo-microscopy". Q. Rev. Biophys. 37: 3–13. doi:10.1017/S0033583504003920. PMID 17390603.
  11. ^ Dr Richard Henderson FRS FMedSci Fellow Profile,Academy of Medical Sciences
  12. ^ a b CV of Richard Henderson
  13. ^ Nouriani, Olivia (6 October 2017). "2 scientists with ties to UC Berkeley win 2017 Nobel Prize in Chemistry". The Daily Californian. Retrieved 10 October 2017.
  14. ^ Dr Richard Henderson FRS FMedSci Fellow Profile,Academy of Medical Sciences
  15. ^ Dr Richard Henderson FRS FMedSci Fellow Profile,Academy of Medical Sciences
  16. ^ Dr Richard Henderson FRS FMedSci Fellow Profile,Academy of Medical Sciences
  17. ^ Announcement of Newly Elected Honorary Members" from the British Biophysical Society
  18. ^ Copley Medal 2016
  19. ^ "The Nobel Prize in Chemistry 2017". The Nobel Foundation. 4 October 2017. Retrieved 6 October 2017.
  20. ^ "Nobel Prize in Chemistry Awarded for Cryo-Electron Microscopy". The New York Times. 4 October 2017. Retrieved 4 October 2017.
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