Barbara Low (biochemist)
Barbara Wharton Low
Low in 1960
|Died||January 10, 2019 (aged 98)|
Riverdale, Bronx, New York, US
|Education||B.A. (1943), M.A. (1946), D.Phil. (1948)|
|Alma mater||Somerville College, Oxford|
|Known for||Discovery of penicillin structure, discovery of pi helix|
|Title||Professor of Biochemistry & Molecular Biophysics|
|Partner(s)||Metchie J. E. Budka|
|Doctoral advisor||Dorothy Hodgkin|
|Notable students||Frederic M. Richards, Helen M. Berman, Clara Shoemaker|
Barbara Wharton Low (March 23, 1920 – January 10, 2019) was a biochemist, biophysicist, and a researcher involved in discovering the structure of penicillin and the characteristics of other antibiotics. Her early work at Oxford University with Dorothy Hodgkin resulted in the first X-ray crystallography deconstruction of the molecular structure of penicillin, the largest molecule ever completed using that method. Later graduate work saw her study with Linus Pauling and Edwin Cohn before becoming a professor in her own right. Low's laboratory would accomplish the discovery of the pi helix, investigate the structure of insulin, and conduct research into neurotoxins.
Childhood and education
Low was born on March 23, 1920 in Lancaster, England to her parents, Matthew Low and Mary Jane Wharton. She undertook her tertiary education at Somerville College, Oxford, graduating with a bachelor's degree in 1943. The same year she began work under the biochemist Dorothy Hodgkin. Due to Hodgkin's focus on protein crystallography, for which she was later awarded a Nobel prize, Low and her academic colleagues were engaged in researching the use of X-rays to determine the structure of crystallized proteins. Low obtained Master's and doctoral degrees in chemistry from Oxford University in 1946 and 1948 respectively, before moving on to a research associate position at the California Institute of Technology (Caltech). To do so, she obtained a United States passport through emigration and later full citizenship in 1956.
While at Caltech, she worked under Nobel Laureate Linus Pauling for a year before moving to another yearly research associate position at Harvard University working with Edwin Cohn. The following year, in 1950, Harvard offered Low her first academic appointment as assistant professor of biophysical chemistry. She relocated to Columbia University in 1956 as an associate professor, and was promoted to a full professorship in 1966. Low continued at Columbia until her retirement in 1990 as professor emerita of biochemistry and molecular biophysics. She still did routine academic rounds as a "Special Lecturer" at the university, however, up until 2013.
During Low's early work with the Hodgkin laboratory in the final years of World War II, she discovered the sulfur elemental components of penicillin that allowed for its mass production and later transformation into other antibiotic compounds. Up to that point, a pure sample of penicillin had not been successfully synthesized due to a lack of understanding of its physical structure of the compound, specifically the variation of its penam core. Due to the size of the protein itself, only careful examination of the X-ray results allowed for any information on the overall construction, but the two finally completed the investigation in 1945. At that time, it was the largest molecule ever to have had its structure determined by crystallography. Because the knowledge Low and Hodgkin obtained was of such importance and the research had been funded by the UK government, however, their work on penicillin remained classified for decades afterwards.
At Harvard, Low turned to topics she would continue in her later positions at Columbia University: the structure and composition of insulin and structural investigations into albumin crystals. Once her Columbia lab was established, Low also included research into neurotoxins on her schedule, including curare and its derivatives. The general protein studies from her lab resulted in 1952 with the discovery of the pi helix, a fundamental structural component of a significant number of proteins.
As a member of the Columbia University committee on affirmative action, Low strongly believed in diversifying the faculty and workstaff at the university. She wished to help improve the standing of women in science and did so in one way by hiring and nurturing a large number of female graduate students in her lab.
Honors and awards
- Crowfoot, D.; Bunn, C.W.; Rogers-Low, B.W.; Turner-Jones, A. (1949). "The X-ray crystallographic investigation of the structure of penicillin". Chemistry of Pencillin. Princeton University Press: 310–367.
- Low, Barbara W.; Baybutt, R. B. (1952). "The π Helix—A Hydrogen Bonded Configuration of the Polypeptide Chain". J. Am. Chem. Soc. 74 (22): 5806–5807.
- "BARBARA LOW Obituary". The New York Times. February 25, 2019. Retrieved March 19, 2019.
- Roberts, Sam (March 13, 2019). "Barbara Low, Whose Research Identified the Shape of Penicillin, Dies at 98". The New York Times. Retrieved March 19, 2019.
- "Barbara Low: Pioneer in X-Ray Crystallography". Columbia University Irving Medical Center. March 5, 2019. Retrieved March 15, 2019.
- Edsall, John T. (1971). "Some Personal History and Reflections from the Life of a Biochemist". Annual Review of Biochemistry. Annual Reviews. 40 (1): 1–29. doi:10.1146/annurev.bi.40.070171.000245. ISSN 0066-4154.
- "Barbara Wharton Low". American Academy of Arts & Sciences. March 27, 2018. Retrieved March 15, 2019.
- Martha J. Bailey: American Women in Science: 1950 to the Present. ABC-CLIO, 1998, p. 241.
- Kalte, Nemeh & Schusterbauer: American Men & Women of Science. 22nd Edition, Volume 4 (J-L), Thomson Gale, 2005, p. 927.