 | Born: February 11, 1929 Professor, Stanford University School of Medicine |
Phone and Fax numbers: Email:
jardetzky@stanford.edu
|
Click to go to:
| Memberships/ Honors | Visiting Appointments | Editorial/Organizational Activities | Publications |
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| 1950 | B.A. in Chemistry and Biology, Macalester College, St. Paul, Minnesota |
| 1953 | M.S. in Physiology, minor in Physiological Chemistry, University of Minnesota |
| 1954 | M.D., University of Minnesota Medical School |
| 1956 | Ph.D. in Physiology and Physical Chemistry, University of Minnesota |
| 1950-54 | Research Assistant in Physiology, University of Minnesota |
| 1954-56 | American Heart Assn. Research Fellow, Physiology Dept., U. Minnesota |
| 1956-57 | National Research Council Fellow, Department of Chemistry, CalTech |
| 1957-59 | Associate in Pharmacology, Harvard Medical School |
| 1959-66 | Assistant Professor of Pharmacology, Harvard Med. School and Senior Fellow, USPHS |
| 1966-68 | Director, Department of Biophysics and Pharm., Merck Institute for Therapeutic Research |
| 1968-69 | Executive Director, Basic Medical Sciences, Merck Institute for Therapeutic Research |
| 1969-94 | Professor of Pharmacology, Stanford University |
| 1973-74 | Acting Chairman, Department of Pharmacology, Stanford University |
| 1972-75 | Chairman, Administrative Committee of the Stanford Magnetic Resonance Laboratory |
| 1975-97 | Director, Stanford Magnetic Resonance Laboratory |
| 1994+ | Professor of Molecular Pharmacology, Stanford University |
| 1997+ | Director Emeritus, Stanford Magnetic Resonance Laboratory |
| Visiting Appointments | Editorial/Organizational Activities | Publications |
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| Memberships/ Honors | Editorial/Organizational Activities | Publications |
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| Memberships/ Honors | Visiting Appointments | Publications |
|---|
| Memberships/ Honors | Visiting Appointments | Editorial/Organizational Activities |
|---|
 | "Flexibilty map of the trp repressor." Rasmol model of the trp repressor as seen from the DNA "viewpoint" with leucine and valine residues shown in space-filling format. The most slowly exchanging residues are on the interior of the core. Finucane and Jardetzky (1996) Protein Science 5, 653-662. Click here to see other recent images from SMRL. |
Keeper of this page: reh@stanford.edu
