John Anthony Schellman

John Anthony Schellman (October 24, 1924–December 16, 2014) was an American biophysical chemist at the University of Oregon, a member of the National Academy of Sciences, a Biophysical Society Fellow, and an American Physical Society Fellow.

Early life and education The son of John A. and Margaret Mary (née Mason) Schellman, John Anthony Schellman was born in Philadelphia on October 24, 1924. He earned an M.A. in 1949 and a Ph.D. in Theoretical Chemistry in 1951, both at Princeton University. His dissertation was titled, The Theory of the Dielectric Properties of Ice, and was advised by Walter Kauzmann.

Career

Post-doctoral fellowship Schellman's first postdoctoral fellowship was a U.S. Public Health Service award from NIH, with Leo Samuels at the University of Utah Medical School, working to improve chemical and biological assays of steroid hormones.

Schellman's ensuing research led to three important developments. First, he "derived an equation to analyze how the number of H-bonds made between urea molecules in water should change when a concentrated urea solution is diluted", yielding measurements suggesting "the peptide H-bond should be marginally stable in water". (She developed the "Schellman motif", on α-helix termination in proteins by a characteristic sequence.) According to Baldwin and von Hippel, "Their ORD results were published in a magnum opus (seven papers on ten proteins) in 1958, after they had left the Carlsberg Lab."

Of Schellman's work at Oregon, Robert Baldwin and Peter von Hippel wrote,

Quote| quote = ...John dug deeper into the problems he had opened up at the Carlsberg Lab and began to analyze the physical properties of DNA. He clarified the foundations of the subjects he studied, especially of circular dichroism and the energetics of protein folding. In 1962 John and his student Patrick Oriel found that the n-pi* transition of the peptide group is responsible for the Cotton effect that is used to measure α-helix formation in ORD studies. (In CD studies, the n-pi* transition is responsible for the 220 nm CD band that is used to measure α-helix content.) ...In the 1970s the study of protein mutants became an important approach to the protein folding problem and John and his coworkers developed methods of analyzing the properties of mutant proteins. John's methods were widely used, both in equilibrium studies of mutational effects on protein stability and in kinetic studies of how mutations affect the rates of protein folding. Referring to his "landmark paper on the stability of the α-helix in 1955", as well as his research and teaching, they commented on his work in the tradition of Linderstrøm-Lang, with his wife Charlotte. Eisenberg said Shellman's contributions included, "fluctuations and linkage relations in macromolecular solutions w25x, a simple model for solvation in mixed solvents w26x, the relation between the free energy of interaction and binding w27x and the thermodynamics of solvent exchange w28x." 1983 American Physical Society Fellow, cited For the application of rigorous physical theory and the development of novel experimental techniques to increase our understanding of the structure and behavior of biological macromolecules, especially proteins and nucleic acids.

1983 Member, American Academy of Arts and Sciences 1983 Honorary Doctorate, Chalmers University, Sweden

1986 Chalmers 150th Anniversary Professorship, Chalmers University, Gothenburg, Sweden 1990 Honorary Doctorate, University of Padua, Italy 2001 Fellow, Biophysical Society