December 2009

Retrospective: Charles Tanford (1921–2009)

 

Charles TanfordCharles Tanford was one of the leaders of that remarkable generation of physical chemists who were drawn to biology in the decade following World War II. Their incursion into biochemistry tilted the emphasis quite abruptly, away from metabolic processes and toward the structure and thermodynamics of macromolecules. From this sprang the effulgent new discipline of molecular biology, viewed with mistrust by many biochemists, for it was, in the words of Erwin Chargaff, no more than “biochemistry practiced without a license.”

Tanford was also a part of the wave of Central European émigrés who so enriched the American academic scene in the 1930s. He was born to assimilated Jewish parents in Halle, Germany. In 1929, his father, Max Tannenbaum, foreseeing perhaps what was to happen five years later, pulled up his roots and took his family to London. The next year, he changed his name to Tanford, and Charles, age 8, was sent to the very reputable University College School. In 1939, Max made another far-reaching decision and dispatched his son to New York into the care of an aunt. Charles’ mother and younger sister eventually followed.

Another relative, at Max’s urging, got Tanford into New York University to study chemistry. On graduating, he was enrolled as a graduate student at Princeton University with the expectation that he would work with one of the leading theoretical chemists of the day, Henry Eyring. However, the war intervened, and Tanford was drafted and sent to Oak Ridge to assist in Harold Urey’s program on the fractionation of uranium isotopes.

When the war was over, Tanford returned to Princeton, but Eyring imposed the condition that he must work with another professor, R. N. Pease, on combustion in gases. This was not what he wanted to study, but the work produced a Ph.D. and two papers on what became known as the Tanford-Pease theory; this enjoyed a brief vogue before being supplanted, according to Tanford, by more elegant formulations.

At this point, chance intervened to change the course of Tanford’s life and career: Walter Kauzmann arrived at Princeton as an assistant professor and ignited Tanford’s enduring fascination with proteins. Rejecting the temptations of a lucrative industrial job, Tanford applied instead for a place in Edwin Joseph Cohn’s protein laboratory— the only one of its kind in the country, and, in its setting at Harvard Medical School, a curious anomaly. When Tanford arrived, the main concern of the laboratory was the rigorous analysis of proteins, in respect of molecular weight, size, charge and ion binding, and it had attracted a galère of distinguished chemists. The most important for Tanford was George Scatchard, for whom he developed a deep admiration and from whom he absorbed the finer points of solution thermodynamics.

After two years, and equipped with a grasp of the mainly hydrodynamic techniques then available for the study of proteins in solution, Tanford headed for his first faculty position in the chemistry department of the University of Iowa. There, he taught a course on the physical chemistry of polymers and discovered that no satisfactory textbooks were available. It was at this point that he resolved to write his own, an undertaking that was to occupy him intermittently for eight years and resulted in the book “Physical Chemistry of Macromolecules.”

In the midst of all this, he took a sabbatical year with eminent theoretician J. G. Kirkwood at Yale University. There, he developed a theoretical treatment of the electrostatic characteristics of globular zwitterionic polyampholytes, based on evenly distributed discrete ionising groups, rather than on the familiar model of a uniformly charged surface. The outcome permitted a realistic interpretation of acid-base titration profiles of proteins, many of which Tanford and his students measured in the laboratory.

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