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College of Arts and Sciences
Member, Texas Tech University System The Princeton Review - 373 Best Colleges, 2011 Edition

Dr. John Jacob Osterhout

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Department of Chemistry and Biochemistry

Professor/Department Chair
  • Postdoctoral: Stanford Medical School (1985–88)
  • Welch Fellow, (1982–85) UTHSC Houston
  • Ph.D., (1981) University of Texas at Austin
  • B.S., (1974) Rice University

CHEM 1301, CHEM 1411, CHEM 4333, CHEM 6383

Protein Folding

My laboratory studies a model peptide, ατα, which is a de novo designed helix-turn-helix peptide. Circular Dichroism (CD) and Nuclear Magnetic Resonance (NMR) are used to study the conformation of this peptide and its variants. The experimental results are described by the extended helix-coil (XHC) model that is an extension of Lifson-Roig theory. The theory allows us to calculate the balance between helix formation and hydrophobic collapse in protein folding.

Venom

My laboratory also studies snake venom and its interaction with antivenom. In an earlier study an undergraduate researcher examined the effects of foaming-induced denaturation on the physical properties and activity of the commercial antivenoms available in North America. My current work concerns the protein components, and their individual and geographic variation in Crotalus atrox (western diamondback rattlesnake) and Agkistrodon piscivorus (Cottonmouth) venoms. I am a member of the VIPER Institute (VIPER = Venom, Immunology, Pharmacology and Emergency Response) in Tucson, Arizona.

  • Xian, W., Connolly, P. J., Oslin, M., Hausrath, A. C. & Osterhout, J. J (2006) Fundamental interactions in protein folding: Measuring the energetic balance between helix formation and hydrophobic interactions. Protein Science 15, 2062-2070.
  • Kanavage, A. D., Boyer, L. V., McNally, J. & Osterhout, J. J. (2006) Renaturation of antivenom proteins after foaming. Toxicon 47, 445-452.
  • Fezoui, Y., Hartley, D. M., Walsh, D. M., Selkoe, D. J., Osterhout, J. J. & Teplow, D. B. (2000) A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils. Nat. Struct. Biol. 7, 1095-1099.
  • Knubovets, T., Osterhout, J. J., Connolly, P. J. & Klibanov, A. M. (1999) Structure, thermostability and conformational flexibility of hen egg-white lysozyme dissolved in glycerol. Proc. Natl. Acad. Sci. USA 96, 1262-1267.
  • Fezoui, Y., Connolly, P. J. & Osterhout, J. J. (1997) Solution structure of ατα, a helical hairpin peptide of de novo design. Prot. Sci. 6, 1869-1877.
  • Fezoui, Y., Weaver, D. L. & Osterhout, J. J. (1995) Strategies and rationales for the de novo design of a helical hairpin peptide. Prot. Sci. 4, 286-295.

Previous Appointments
Research associate professor, Biochemistry and Molecular Biophysics Department, University of Arizona, Tucson, Ariz. (2002–08)
Head of the protein folding and design group, The Rowland Institute for Science, Cambridge, Mass. (1988–2001)

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