William Astbury

William Thomas Astbury FRS (25 February 1898 – 4 June 1961) was an English physicist and molecular biologist who made pioneering X-ray diffraction studies of biological molecules. His work on keratin provided the foundation for Linus Pauling's discovery of the α-helix. He also studied the structure for DNA in 1937 and made the first step in the elucidation of its structure.

Astbury was the fourth child of seven, born in Longton, Stoke-on-Trent. His father, William Edwin Astbury, was a potter and provided comfortably for his family. Astbury also had a younger brother, Norman, with whom he shared a love of music.^{[citation needed]}

Astbury might well have become a potter but, luckily, won a scholarship to Longton High School, where his interests were shaped by the Headmaster and second master, both chemists. After becoming head boy and winning the Duke of Sutherland's gold medal, Astbury won the only local scholarship available and went up to Jesus College, Cambridge.^{[citation needed]}

After two terms at Cambridge, his studies were interrupted by service during the First World War. A poor medical rating following appendectomy resulted in his posting in 1917 to Cork, Ireland with the Royal Army Medical Corps. He later returned to Cambridge and finished his last year with a specialization in physics.

After graduating from Cambridge, Astbury worked with William Bragg, first at University College London and then, in 1923, at the Davy-Faraday Laboratory at the Royal Institution in London. Fellow students included many eminent scientists, including Kathleen Lonsdale and J. D. Bernal and others. Astbury showed great enthusiasm for his studies and published papers in the journal Classic Crystallography, such as on the structure of tartaric acid.

In 1928, Astbury was appointed Lecturer in Textile Physics at the University of Leeds. He remained at Leeds for the remainder of his career, being appointed Reader in Textile Physics in 1937 and Professor of Biomolecular Structure in 1946. He held the chair until his death in 1961. He was elected a Fellow of the Royal Society (FRS) in 1940. He is commemorated by the Astbury Centre for Structural Molecular Biology at Leeds.

In later life he was given many awards and honorary degrees.

At Leeds Astbury studied the properties of fibrous substances such as keratin and collagen with funding from the textile industry. (Wool consists of keratin.) These substances did not produce sharp patterns of spots like crystals, but the patterns provided physical limits on any proposed structures. In the early 1930s, Astbury showed that there were drastic changes in the diffraction of moist wool or hair fibres as they are stretched significantly (100%). The data suggested that the unstretched fibres had a coiled molecular structure with a characteristic repeat of 5.1 Å (=0.51 nm). Astbury proposed that (1) the unstretched protein molecules formed a helix (which he called the α-form); and (2) the stretching caused the helix to uncoil, forming an extended state (which he called the β-form). Although incorrect in their details, Astbury's models were correct in essence and correspond to modern elements of secondary structure, the α-helix and the β-strand (Astbury's nomenclature was kept), which were developed twenty years later by Linus Pauling and Robert Corey in 1951. Hans Neurath was the first to show that Astbury's models could not be correct in detail, because they involved clashes of atoms. Neurath's paper and Astbury's data inspired H. S. Taylor (1941,1942) and Maurice Huggins (1943) to propose models of keratin that are very close to the modern α-helix.