Her death was confirmed by Lucky Tran, a spokesman for the Irving Medical Center of Columbia University, where Low taught for nearly 60 years and was professor emeritus of biochemistry and molecular physics. Her death was announced belatedly because it took time for the university to gather biographical details, Tran said.
Low’s role in identifying the structure of penicillin was something of a fluke.
As a student at Oxford University in England, she was a protégée of the future Nobel laureate Dorothy Crowfoot Hodgkin, who, having been barred from teaching men, taught at Oxford’s Somerville College, a women’s school at the time.
At Somerville, Hodgkin was a founder of protein crystallography, a process that can determine a molecule’s three-dimensional shape by analyzing how X-rays bend and bounce off its crystallized form. She trained a cadre of students, including Barbara Low, in the emerging field.
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“Red-hot news,” Low told Hodgkin in July 1943, according to the book “Dorothy Hodgkin: A Life” (2014), by Georgina Ferry. “Penicillin and all its degradation products contain sulfur. This is very hush-hush.”
Their wartime research helped transform penicillin — the bacteria-killing substance that Alexander Fleming had discovered in mold in 1928 — into a wonder drug that could be replicated, mass-produced and reconfigured to produce stronger antibiotic derivatives for the treatment of a broader range of infections.
Hodgkin had begun her career in 1932 in the laboratory of John Desmond Bernal, a pioneer in X-ray crystallography, at the University of Cambridge in England. At Oxford, she and Low focused on penicillin, which was first used to treat humans in 1941.
Chemists were still trying to isolate pure penicillin so it could be studied and synthesized. They used rudimentary computers. But as Ernst B. Chain, their colleague at Oxford, later said, “The final solution of the problem of the structure of penicillin came from crystallographic X-ray studies.”
Hodgkin received the Nobel Prize in Chemistry in 1964 for her breakthrough research in crystallography. The award citation went beyond her work in penicillin to mention her subsequent determination of the crystal structure of vitamin B-12 and other substances that proved vital in advancing medical care.
Barbara Wharton Low was born on March 23, 1920, in Lancaster, in northwestern England, to Matthew and Mary Jane (Wharton) Low. She graduated from Sommerville with a bachelor’s degree in chemistry in 1943 and later received her master’s and doctorate in chemistry from Oxford.
After emigrating to the United States (she became a citizen in 1956), she was a research assistant to Linus C. Pauling, another future Nobel laureate, at the California Institute of Technology, and to biochemist Edwin Cohn at Harvard. In 1950 she was appointed an assistant professor of biophysical chemistry at Harvard, where she discovered a protein structural element in amino acids known as the pi helix.
Low joined the Columbia faculty as an associate professor in 1956 and was promoted to professor in 1966. Her research there led to a better understanding of the protein receptor that responds to the neurotransmitter targeted by snake venom.
She retired as a professor in 1990, but she continued to lecture at the university until 2013.
Her legacy at Columbia went beyond academics: It was grounded in a commitment to rectify the second-class treatment her mentor had received as a teacher at Oxford.
“On the university’s affirmative action committee, she was very forceful in wanting Columbia to live up to its ideals of having a diverse faculty and work force,” Arthur G. Palmer, a professor of biochemistry and molecular biophysics and associate dean for graduate affairs at Columbia’s medical center, said in an email.
In 1950 Low married Metchie J.E. Budka, a fellow biochemist whom she had met at Harvard. He died in 1995. A sister, Marjorie Elizabeth Camp, died in 2002. No immediate family members survive.
This article originally appeared in The New York Times.