Edith Wilson Miles

Miles received her B.A. from the University of Texas at Austin in 1957, and then moved to the University of California, Berkeley where she earned a Ph.D. in 1962[1] working in Esmond Emerson Snell's lab with Jesse Rabinowitz and Edward Adelberg as her advisors.[2][3] With funding from the American Cancer Society, she moved to the University of Leicester as a postdoctoral researcher with Hans Kornberg. From 1964 until 1966, she was a postdoctoral investigator at Tufts University working with Alton Meister, and then she accepted an independent position at the National Institutes of Health. In 2000 she became a Scientist Emeritus.[1]

Wilson's graduate research characterized an enzyme that required pyridoxal phosphate and tetrahydrofolate to convert α-methylserine to alanine and formaldehyde.[4][5] Her subsequent work examined the glyoxylate cycle in bacterial cells and led to further investigation of enzymes that require pyridoxal phosphate.[6] Upon her move to the National Institutes of Health, she began to focus on tryptophan synthase,[7][8][9] first by establishing the mechanism of the enzyme[10] which would later allow her to investigate interactions between the subunits of the enzyme.[1] Wilson went on to use x-ray crystallography to obtain the structure of the enzyme,[11][12] and used mutant forms of Salmonella typhimurium to identify the significant components of the enzyme.[1] She also showed that α₂β₂ complex of tryptophan synthase could unfold in the presence of guanine hydrochloride,[13] details about protein folding and shape that became relevant in later research about barrel-shaped proteins.[14][15]

• Wilson, EM; Kornberg, HL (September 1, 1963). "PROPERTIES OF CRYSTALLINE l-ASPARTATE 4-CARBOXY-LYASE FROM ACHROMOBACTER SP". Biochemical Journal. 88 (3): 578–587. doi:10.1042/bj0880578. ISSN 0006-2936. PMC 1202217. PMID 14071532.
• Hyde, C C; Ahmed, S A; Padlan, E A; Miles, E W; Davies, D R (1988). "Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium". Journal of Biological Chemistry. 263 (33): 17857–17871. doi:10.1016/s0021-9258(19)77913-7. ISSN 0021-9258. PMID 3053720.
• Miles, Edith Wilson (1991). "Structural basis for catalysis by tryptophan synthase". Advances in enzymology : and related areas of molecular biology. Vol.64. Vol. 64. Internet Archive. New York ; Chichester : Wiley. pp. 93–172. ISBN 978-0-471-50949-3.
• Miles, Edith Wilson; Rhee, Sangkee; Davies, David R. (1999). "The Molecular Basis of Substrate Channeling". Journal of Biological Chemistry. 274 (18): 12193–12196. doi:10.1074/jbc.274.18.12193. PMID 10212181.
• Miles, Edith Wilson (April 5, 2013). "The Tryptophan Synthase α2β2 Complex: A Model for Substrate Channeling, Allosteric Communication, and Pyridoxal Phosphate Catalysis". Journal of Biological Chemistry. 288 (14): 10084–10091. doi:10.1074/jbc.X113.463331. ISSN 0021-9258. PMC 3617248. PMID 23426371.

While at the University of Texas at Austin, Miles (then known as Edith Margaret Wilson) was inducted into Alpha Lambda Delta,[16][17] an honor society that recognizes achievement of first year university students and for which she later served as secretary.[18] In her senior year, 1957, she was elected to Phi Beta Kappa[19]^: 170and was a member of Mortar Board.[19]^: 189 In 1994, Miles received the Hillebrand Award, named for William Francis Hillebrand, from the Chemical Society of Washington, a section of the American Chemical Society.[20]

Her husband, H. Todd Miles, also worked at the National Institutes of Health and became Scientist Emeritus in 2000.[1]