Jane Shelby Richardson

Jane Shelby Richardson (born January 25, 1941) is an American biophysicist best known for developing the Richardson diagram, or ribbon diagram, a method of representing the 3D structure of proteins. Ribbon diagrams have become a standard representation of protein structures that has facilitated further investigation of protein structure and function globally. With interests in astronomy, math, physics, botany, and philosophy, Richardson took an unconventional route to establishing a science career. She attended Teaneck High School and in 1958 won third place in the Westinghouse Science Talent Search, the most prestigious science fair in the United States, with calculations of the satellite Sputnik's orbit from her own observations.

She continued her education intending to study mathematics, astronomy and physics at Swarthmore College. However, Richardson instead graduated Phi Beta Kappa with a bachelor's degree in philosophy and a minor in physics in 1962 before she pursued graduate work in philosophy at Harvard University. Meanwhile, she was able to enroll in plant taxonomy and evolution courses at Harvard that would later contribute to her big-picture approach to studying protein structure. Since Harvard's philosophy focused on modern philosophy instead of Richardson's interest, classical philosophy, Richardson left with her master's degree from Harvard in 1966. Post-graduation, Richardson tried teaching high school, but soon realized that this career path was not for her. She subsequently rejoined the scientific world, working as a technician at Massachusetts Institute of Technology in the same laboratory as her husband, David Richardson, whom she met at Swarthmore College. Over the course of her career, Richardson has been recognized by many prestigious institutions of the scientific community. In July 1985 she was awarded a MacArthur Fellowship for her work in biochemistry. She was elected to the National Academy of Sciences and the American Academy of Arts and Sciences in 1991 and to the Institute of Medicine in 2006. ). For the 2012-2013 year, Richardson was elected president of the Biophysical Society for the 2012-2013 year, and she became a fellow of the American Crystallographic Association in 2012. Richardson is currently a James B. Duke Professor of Biochemistry at Duke University.

Scientific work and contributions Richardson's first forays into science were in the field of astronomy. By observing the position of Sputnik – at the time, the only artificial satellite – on two successive nights, she managed to calculate its predicted orbit. She submitted her results to the Westinghouse Science Talent Search, winning third place in 1958.

Richardson joined her husband David C. Richardson, then completing his PhD work at MIT, in studying the 3-dimensional structure of the staphylococcal nuclease protein (1SNS) by X-ray crystallography for his doctoral thesis. Staphylococcal nuclease was among the first dozen protein structures solved. Classes in botany and evolution that she had taken while pursuing her degree shaped her thinking about the work she was doing in the chemistry laboratory. By 1977 she published her findings on protein relatedness in Nature, with a paper entitled "β-sheet topology and the relatedness of proteins".

As Richardson developed the ribbon diagram to illustrate her findings over the course of her taxonomic research, her iconic images first appeared in the review journal Advances in Protein Chemistry in an article titled "The anatomy and taxonomy of protein structure" 1981, an early hallmark publication in structural bioinformatics. The diagrams have since become a standard way of visualizing protein structure, specifically depicting beta-sheet topology and connections between amino acid sequences, or peptides, that make up proteins. The protein folding process involves four levels: primary structures, secondary structures, tertiary structures, and quaternary structures. Secondary structures result from hydrogen bond interactions between adjacent amino acids sequences to form alpha helices or beta-sheets. Tertiary structures are a higher order of protein folding that depict the conformation of and connectivity between alpha-helices and beta-sheets in 3D. Her initial drawings and continual discoveries contribute to a broader understanding of protein energetics and evolution. Peter Agre, Nobel laureate and fellow Duke professor, said of the Richardsons' work: "Jane and David’s work allowed us to reveal the form of proteins, and from there it was easier to understand their function". In the 1990s the Richardsons developed the kinemage system of molecular graphics and David Richardson wrote the Mage program to display them on small computers, for the then-new journal Protein Science. Additionally, they developed all-atom contact analysis (see image) to measure "goodness of fit" inside proteins and in interactions with surrounding molecules. Fundamentals of Biochemistry by Viet, Voet & Pratt, Principles of Biochemistry by Horton et al., and the University of Mississippi's Kinemage Authorship Project.

The Richardson Laboratory currently studies structural motifs in RNA as well as proteins, as part of the RNA Ontology Consortium (ROC) to better communicate RNA structure and function research findings. The laboratory has acted as assessors in the CASP8 structure-prediction experiment (CASP), is one of the four developer teams on the PHENIX software system for x-ray crystallography of macromolecules, and hosts the MolProbity web service for validation and accuracy improvement of protein and RNA crystal structures. MolProbity uses the KiNG program (successor to Mage) for showing 3D kinemage graphics on-line. Jane Richardson serves on the worldwide Protein Data Bank (wwPDB) X-ray Validation Task Force and NMR Validation Task Force. As she continues to run the Richardson laboratory alongside her husband at Duke, where they use MolProbity to validate RNA, protein, crystal structures, she also adds science-related images, images of nature, and pictures for the WikiProject Biophysics to Wikimedia Commons. 1991: Election to National Academy of Science, an honor that recognizes exceptional previous and continual original research 2006: Election to the National Academy of Medicine in Washington, D.C., a nonprofit institution that strives to offer objective science, technology, and health advice 2012: American Crystallographic Association fellow in 2012 for fulfilling the following criteria: "a Member whose efforts on behalf of the advancement of crystallography or its applications that are scientifically or socially distinguished" 2012 - 2013: President of the Biophysical society 2019: Alexander Hollaender Award in Biophysics, an award of distinguished biophysics contributions

Notable publications The following articles are classified as highly cited in field by Web of Science as of February 17, 2020: