[Linus Pauling]

Linus Pauling and Robert Corey at Caltech; Offered by the estate of American Biochemist Richard E. Dickerson (1931-2025), Distinguished Professor, Director of the Molecular Biology Institute at UCLA from 1983-1994, elected to the National Academy of Sciences and American Academy of Arts and Sciences in 1985. Exhibited at UCLA’s Molecular Biology Institute.

The present pair of models, inherited from Linus Pauling and Robert B. Corey’s laboratory, demonstrate two of Pauling and Corey’s fundamental chain-folding components of protein structures that they proposed in 1951: the antiparallel and parallel beta pleated sheet. In an exhibition description made by Professor Dick Dickerson he pointed out that “Pauling’s greatest single contribution to protein structure was the realization that peptide groups had to be planar because of the partial double-bond character of their central C-N bond.”

The models were constructed with parts that Pauling had custom made in the Caltech chemistry machine shop. He mentioned the new model pieces in a September 14, 1954 letter to his son Peter: “Did I tell you that we have made some more dural models, in which the bond angles and bond distances are exactly right for an ordinary amide group? We have also made some in which the angles have the right values for a proline residue. I decided the other day that these models are with us to stay, and that we should order 10,000 Allen set screws, for $227, in order to get the reduction in price. This is enough for about 100 models, each with about 25 amino-acid residues in it” (OSU Pauling Day-by-Day). The “dogbone” pieces represent “a structurally accurate model of the peptide group that connects two amino acid residues: -CO-NH-“ (Dickerson, exhibition text).