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George D. Rose, Ph.D.
Krieger-Eisenhower Professor Emeritus, Krieger School of Arts and Sciences, Johns Hopkins University
Joint Appointment in Biophysics and Biophysical Chemistry
Research Interests: Protein folding
Dr. George D. Rose holds a joint appointment in biophysics and biophysical chemistry at the Johns Hopkins University School of Medicine. He is the Krieger-Eisenhower Professor Emeritus in the Thomas C. Jenkins Department of Biophysics in the Krieger School of Arts and Sciences at Johns Hopkins. His research focuses on protein folding.
His team is currently studying the spontaneous disorder order transition that occurs in proteins under certain physiological conditions.
Dr. Rose received his undergraduate degree in mathematics in 1963 from Bard College. He earned his M.S. in mathematics and computer science from Oregon State University in 1972, and his Ph.D. In biochemistry and biophysics from Oregon State University in 1976.
Prior to joining Johns Hopkins, Dr. Rose was Alumni Endowed Professor of Biochemistry and Molecular Biophysics at Washington University School of Medicine in St. Louis, MO. From 1991-92, he was a professor in the Department of Biochemistry and Biophysics at the University of North Carolina, Chapel Hill. From 1980-91 he was distinguished professor in the Department of Biological Chemistry at the M.S. Hershey Medical Center of The Pennsylvania State University.
His work was recognized in 2014 with a Temporary Eminent Scholar appointment in the department of chemistry faculty at the Technische Universität München. In 2011, he became Honorary Hans Fischer Senior Fellow at the Institute for Advanced Study, Technische Universität München. In 2011 he also received the Humboldt Research Award (Forschungspreise).
- Krieger-Eisenhower Professor Emeritus, Krieger School of Arts and Sciences, Johns Hopkins University
- Joint Appointment in Biophysics and Biophysical Chemistry
Departments / Divisions
Research & Publications
Dr. Rose’s research is focused primarily on protein folding, the spontaneous disorder order transition that occurs under physiological conditions. The protein polymer is flexible when unfolded but adopts its unique native, three dimensional structure when folded.
Lab Website: George Rose Lab
George D. Chellapa and George D. Rose. "On interpretation of protein X-ray structures: planarity of the peptide unit." Proteins, Structure, Function and Bioinformatics, 83: 1687-1692. 2015.
Robert L. Baldwin and George D. Rose. "Frederic Richards: a NAS biographical memoir." 2014.
Robert L. Baldwin and George D. Rose. "Molten globules, entropy-driven conformational change and protein folding." Curr Opin Struct Biol 23:4-10. 2013.
George D. Rose. "The open-ended intellectual legacy of GNR." Biomolecular Forms and Function, World Scientific Publishing, Singapore, 2013.
George D. Chellapa and George D. Rose. "Reducing the dimensionality of the protein-folding search problem." Protein Science 21:1231-1240. 2012.
Activities & Honors
- Temporary Eminent Scholar, Faculty of the Technische Universität München, Department of Chemistry, 2014
- Honorary Hans Fischer Senior Fellow, Institute for Advanced Study, Technische Universität München, 2011
- Humboldt Research Award (Forschungspreise), Alexander von Humboldt Foundation, Germany, 2011
- Exceptional Lecturer, Feinberg Teaching Survey, Weizmann Institute Student and Fellows Council, 2010
- Academy of Distinguished Engineers, Oregon State University, 2008
- Fellow, American Association for the Advancement of Science, (AAAS), 2005
- Krieger-Eisenhower Professor, Johns Hopkins University, 2004
- Fellow, John Simon Guggenheim Memorial Foundation, 2002
- John and Samuel Bard Award in Medicine and Science,, Bard College, 1999
- Hinkle Award & Lectureship, Hinkle Society of Pennsylvania State University, 1985
- Research Career Development Award, National Institutes of Health, 1980 - 1985
- Honorary Associate in Computer and Information Sciences, American Museum of Natural History, 1966 - 1969