Professor Dunker received a B.S. degree in Chemistry from the University of California, Berkley, in 1965. He attended the University of Wisconsin at Madison where he earned his M.S. degree in Physics in 1967, and his Ph.D. in Biophysics in 1969. In 1973, he completed a postdoctoral fellowship in Molecular Biophysics from Yale University. He joined Sloan Kettering in 1973 as a Research Assistant. In 1975, he became as Assistant Professor in Biochemistry at Washington State University, where he rose to the rank of Professor in 1983. Professor Dunker joined the faculty of Indiana University School of Medicine in July of 2003 as Professor of Biochemistry and Molecular Biology. He launched and became Director of the Center for Computational Biology and Bioinformatics (CCBB). In July 2004, he became a Consultant with Molecular Kinetics, Inc. In addition to his administrative activities in developing the CCBB, he was named Director of the Bioinformatics Program in the School of Informatics on both the Indianapolis and Bloomington campuses in August of 2006. Dunker's area of expertise involves understanding intrinsically disordered proteins using bioinformatics approaches and laboratory experiments. His research in computational biology and bioinformatics began in the mid-1980's. In the mid-1990's, he used bioinformatics to study intrinsically disordered proteins. He and his collaborators were the first to consider these proteins as a distinct class with important biological functions. His bioinformatics research goals over the next several years included the improvement of intrinsic disorder predictions, especially with respect to identifying different types of disorder (flavors) and then to understanding the relationships between the different types of disorder and protein function, i.e., to understand flavor-function relationships. In addition, he wants to combine bioinformatics prediction with laboratory experimentation to develop new approaches for understanding protein-protein and protein-nucleic acid signaling interactions that involve intrinsically disordered proteins. Ongoing work suggests that the original proteins on earth were intrinsically disordered and that protein evolution followed a disorder to order pathway.