Richard Henderson (biologist)
Richard Henderson ( born July 19, 1945 in Edinburgh, Scotland ) is a British structural and molecular biologist.
Life
Henderson acquired in 1966 from Edinburgh University a bachelor's degree in physics in 1969 at Cambridge University, a Ph.D. in molecular biology. 1969/1970 he worked as a Research Assistant in the Laboratory of Molecular Biology (LMB ) of the Medical Research Council ( MRC) in Cambridge, before he worked as a postdoctoral fellow at Yale University, 1970-1973. His further academic career spent Henderson again at the LMB, most recently (1986-2006) as successor of Aaron Klug as head of the department. Under Henderson's line working simultaneously to about 400 people in the LMB. Among them were the Nobel laureate César Milstein, Georges Kohler and John E. Walker.
Work
Henderson is considered a pioneer of electron microscopy in determining the molecular structure of membrane proteins. He was able to create high-resolution ( 7 Angstroms) maps of the structure of bacteriorhodopsin, with whose help he was able to propose a detailed mechanism of this proton pump, the first insight into the functioning of the proteins of membrane transport.
Together with Nigel Unwin and building on the work of Aaron Klug and Jacques Dubochet explored Henderson at the Laboratory of Molecular Biology (LMB ) of the Medical Research Council various membrane proteins, with Unwin focused on ion channels and Henderson on proteins consisting of seven α -helices including the bacteriorhodopsin and the G- protein-coupled receptor. While Henderson employed at the beginning of his scientific career with X-ray crystallography, the switch provided on the electron has the advantage of being able to examine a protein crystal, which consists of only about 5,000 molecules - for X-ray crystallography four to five orders of magnitude larger crystals are needed.
Further work Hendersons are concerned with the improvement of the electron microscopic technique to ultimately be able to analyze membrane molecules in non- crystalline form.