Richard Henderson is a celebrated molecular biologist and biophysicist, widely regarded as a pioneer in the field of electron microscopy for biological molecules. His research has become an invaluable contribution to world science, and many of the methods he developed are now standard practice for modern scientists. Find out more at edinburghname.
Henderson’s work has been recognised with numerous awards, but the most significant is undoubtedly the 2017 Nobel Prize in Chemistry, which he shared for developing cryo-electron microscopy.
Early Years and Education
The future scientist was born on 19 July 1945 in Edinburgh. He received his primary and secondary education at Newcastleton Primary School, Hawick High School, and finally Boroughmuir High School in Edinburgh. After finishing school, he decided to pursue physics at the University of Edinburgh, earning a bachelor’s degree with first-class honours in 1966.
Henderson was not content to stop there, so he became a postgraduate student at Corpus Christi College, Cambridge. In 1969, he was awarded his PhD.
The Beginning of His Research
Henderson’s first major research project focused on the structure and mechanism of the enzyme chymotrypsin, the results of which were used for his doctoral thesis. However, his true interest lay in membrane proteins. This passion led to an invitation to Yale University as a postdoctoral fellow, where he worked on voltage-gated sodium channels.
A Landmark Publication
The year 1975 marked the beginning of an exciting collaboration between Richard Henderson and Nigel Unwin at the MRC Laboratory of Molecular Biology in Cambridge. Together, they studied the structure of the membrane protein bacteriorhodopsin using electron microscopy. Subsequently, Henderson and Unwin published a paper in the journal Nature that presented a structural model of bacteriorhodopsin, revealing that the protein was composed of seven transmembrane helices.
The publication of this article caused a real sensation in the scientific community. This was not only because the work provided direct proof that membrane proteins had a well-defined structure, but also because it demonstrated for the first time that transmembrane alpha-helices could exist.
Achieving an Atomic Model
Following his successful collaboration with Unwin, Henderson decided to continue studying the structure of bacteriorhodopsin independently. After years of sustained research, repeated verification of his results, and the use of various methods, he once again amazed the scientific community in 1990. That year, Henderson presented an atomic model of bacteriorhodopsin, this time using the technique of electron crystallography.
This achievement is considered only the second atomic model of a membrane protein ever produced. The entire methodology that Henderson developed for electron crystallography continues to be successfully used by scientists today.
A Powerful Partnership
Richard’s career is filled with brilliant, precise, and highly valuable research that has produced incredible results, with each project earning the admiration of his colleagues. Whether working alone or in tandem with other scientists, Henderson always managed to create something extraordinary.
In another successful collaboration, he worked with Chris Tate to develop conformational thermostabilisation, a method that allows any protein to be stabilised while preserving a chosen conformation. The significance of this method proved to be enormous in determining the structures of several G protein-coupled receptors (GPCRs).
From Lab to Lifesaving Drugs
Given the highly successful results of their work, Henderson and Tate decided to take it to the next level, allowing their method to work for the benefit of humanity. In 2007, they co-founded the MRC startup Heptares Therapeutics Ltd (HTL), which uses their technique to develop new drugs. These drugs target GPCRs, which are linked to a wide spectrum of human diseases.
Perfecting Single-Particle Microscopy
Single-particle electron microscopy formed the basis of Henderson’s subsequent independent research. He was one of the earliest advocates for the idea that this technique could be used to determine atomic-resolution models of proteins. Furthermore, Richard was a scientist who dedicated maximum effort to obtaining atomic structures without the need for crystals.
His contribution to the development of numerous tools and methods used in single-particle electron microscopy simply cannot be overstated. This includes his pioneering work on direct electron detectors. Richard was the scientist who first proposed this clever solution, which made the study of samples at cryogenic temperatures significantly more effective and straightforward.
Thus, Richard Henderson is a scientist who can rightly be considered one of the founders of the electron microscopy of biological molecules. Each of his developments became a major event in the scientific community, and the continued use of his methods by modern scientists is the best proof of the talent of this outstanding native of Edinburgh.