Jane and David Richardson Papers

Jane and Dave Richardson with their son

The Archives is happy to announce they are now home to the Jane and David Richardson Papers. Both Jane and David are currently professors in Duke’s Department of Biochemistry. Jane is James B. Duke professor of Biochemistry and David is professor of Biochemistry and founding director of Duke’s Structural Biology and Biophysics Graduate Training Program. The Richardson’s met while students at Swarthmore College. Following graduation, they married and David continued his studies at the Massachusetts Institute of Technology, pursing a PhD in chemistry while working in the laboratory of Albert F. Cotton and researching small molecule inorganic chemistry and crystallography. Meanwhile, Jane attended Harvard University to earn a MA in philosophy and master’s in teaching in 1966. In 1964 Jane became a technician in the same lab where David was conducting his graduate research, beginning the Richardsons’ career long scientific collaboration. The Richardsons began working to solve the structure of the staphylococcal nuclease, an enzyme that cleaves DNA and RNA. At this time, only two proteins had been solved (hemoglobin and myoglobin) and protein crystallography was in its infancy. They determined the structure of the nuclease in 1969, making it the tenth protein structure to be determined. David received his PhD from the Massachusetts Institute of Technology in 1968. The Richardsons then spent at a year at the National Institutes of Health (NIH) before coming to Duke University in 1970.
 
Rhizopuspepsin domain 1Upon their arrival to Duke, David and Jane Richardson established a lab and began working on the structure of copper, zinc superoxide dismutase, an enzyme that protects all living things against the toxicity of oxygen. In the 1980s the Richardsons started exploring synthetic biochemistry and computational biology and helped open up the field of protein de novo design. During the course of their work, the Richadsons designed and made synthetic proteins. These synthetic proteins reveal a great deal about how natural proteins function. In the 1990s, the Richardsons pioneered molecular graphics for personal computers by developing the kinemage system of molecular graphics and the Mage program to display them on small computers, and they developed all-atom contact analysis to measure goodness of fit inside proteins and in interactions with surrounding molecules. In the 2010s, the Richardson lab studied structural motifs in RNA and proteins as part of the RNA Ontology Consortium. The Richardson lab also collaborated in development of the Phenix software suite for X-ray crystallography and hosted the MolProbity, a structure-validation web service that provides broad-spectrum solidly based evaluation of model quality for proteins and nucleic acids. Jane describing documents to Caroline
 
Jane Richardson is widely recognized for her creation of ribbon drawings to schematize protein three-dimensional structures, first published in “Advances in Protein Chemistry” in 1981. The drawings stemmed from Jane’s realization that a general classification scheme could be developed from the recurring patterns of structural motifs within the “folds” of proteins. She created ribbon drawings of those folds, making a uniform set of conventions for drawing the seventy-five protein structures that had been solved at that time. The drawings have been used widely in computer adaptations, and her 1981 paper continues to be cited.
 
The collection primarily consists of drawings, notes, computer printouts and visualizations, and prints pertaining to the Richardsons’ work and research while at Duke University. Major subjects include the structure of copper, zinc superoxide dismutase, protein de novo design, the Protein Data Bank, and 1981 textbook chapter “The Anatomy and Taxonomy of Protein Structure.” To learn more about these materials, visit the finding aid or contact the archives staff. For more information about the Richardsons, Jane’s oral history interview is available upon request at the Archives.
 
This blog was contributed by Archives Intern Caroline Waller.

 

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