
Bob Root-Bernstein is a scientist, humanist, and artist at Michigan State University. He earned his A.B. in Biochemistry (with Bob Langridge in 1975) and Ph. D. in History of Science (with Thomas Kuhn in 1980) from Princeton University. He combined his two fields as a Post-doctoral Fellow in Theories in Biology with Jonas Salk, M. D., at the Salk Institute for Biological Studies. A MacArthur Fellowship (1981-1986) encouraged his multidisciplinary activities. He is currently a Professor of Physiology at Michigan State University where he studies prebiotic evolution, the emergence of interactomes, the evolution of metabolic control systems, autoimmune diseases, drug development, and the creative process in the sciences and arts. The latter endeavour has led to a collaboration with the trans-media artist Adam W. Brown (http://adamwbrown.net) who has helped to design two origins-of-life art exhibits that work simultaneously as open-source scientific experiments, “Origins of Life, Experiment 1.X” and “ReBioGeneSys” (see Figure below). These exhibits have appeared in art galleries and science museums around the world. They are also a way to explore ideas developed with Vic Norris in Rouen, France, that shift the focus of prebiotic evolution from the emergence of specific chemicals or genes to the production of complex chemical ecosystems capable of supporting the emergence of distributed interactomes. Bob also collaborates with his daughter, Meredith Root-Bernstein, on re-imagining the ribosome as the first self-replicating “organism”, an idea that revolutionizes our ideas about ribosomal RNA by making it the original “genome” capable of generating all of the transfer RNAs and messenger RNAs required to produce the ribosomal proteins involved in a functional ribosome. They are currently exploring the origins of the ribosome itself through the integration of a previously distributed ecosystem of virus-like entities that might have arisen through a Norris-type chemical ecosystem composed of RNA fragments (tRNA-like?) that encoded their own self-binding, functionally active peptides connected through mutual catalytic networks.