Member-only story
Nobel Prize Stories by High School Students- Dr. Richard Henderson-A Glimpse of Cellular Infrastructure -Chemistry 2017.
(This article is a summary of the full-length article Authored by Mr. Ketan Tamirisa, South Lakes, TX, USA. It’s one of the 14 Chapters written by high school students and published in the PATH TO NOBEL book).
The book can be purchased at -https://www.afhdusa.org/item/5/path-to-nobel
This chapter presents a detailed profile of Ketan Tamirisa, a junior at Carroll ISD, a public school in Southlake, Texas. Ketan is passionate about writing and reading books and is involved in several projects aimed at supporting educational endeavors and combating poverty in India and the USA. One of the highlights of his high school journey was writing the story and interviewing Dr. Richard Henderson for this book.
The chapter then delves into the life and work of Dr. Richard Henderson, a scientist who revolutionized the field of structural biology with his work on electron cryo-microscopy. Born on July 19, 1945, in Edinburgh, Scotland, Henderson grew up in rural Scotland. He was interested in math and science from a young age and pursued physics at Edinburgh University for his undergraduate studies. For his Ph.D., he attended the University of Cambridge, MRC Laboratory of Molecular Biology.
After obtaining his Ph.D., Henderson worked as a postdoc fellow at Yale for three years before rejoining the MRC laboratory in 1973 as a faculty researcher. His primary focus was on bacteriorhodopsin, a transmembrane protein that captures light energy and uses it to transport protons across the cell membrane.
Henderson’s breakthrough came when he developed a variation of electron microscopy called high-resolution electron cryomicroscopy (cryoEM) imaging. This technique allowed him to produce a high-resolution atomic model of bacteriorhodopsin, revealing that it had seven transmembrane alpha helices across the cell membrane. This was the second membrane protein whose structure was resolved at high resolution.
Over the next twenty years, the techniques were further developed to improve the imaging process, leading to “single particle cryo-EM.” This has now become the principal method to determine the molecular structures of biological proteins. These methods do not require the crystallization of the protein of interest. Instead, the specimens to be studied are placed in “vitreous ice” and studied with electron microscopy, with the images processed with computer power to generate high-resolution final images.
Henderson’s work has had far-reaching implications, particularly for the development of pharmaceuticals. By providing a better understanding of the relationship between structure and function, it has become possible to specifically target medicines to activate or block specific sites on proteins, disrupting or enhancing their functions. Numerous companies have embraced this field to develop new drugs, including numerous anti-HIV drugs.
