Monday, 23 October 2017

Richard henderson

Henderson worked on the structure and mechanism of chymotrypsin for his Ph.D. with David Blow at the MRC Laboratory of Molecular Biology. 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)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.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 not in citation given] This method has been critical in crystallising and solving the structures of several G protein–coupled receptors (GPCRs).With help from the charity LifeArc, Henderson and Tate founded the MRC start-up company, Heptares Therapeutics Ltd (HTL) in 2007. HTL continues to develop new drugs targeting medically important GPCRs linked to a wide range of human diseases.

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, Henderson aims to be able to routinely obtain atomic structures without crystals. 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.

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