Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • Ph.D., University of Oregon 1986
• 

  Previous Appointments & Affiliations

  • Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 1990 - 2019
  • Associate Professor of Biochemistry with tenure, Biochemistry, Basic Science Departments 1997 - 2011
  • Associate Professor of Chemistry, Chemistry, Trinity College of Arts & Sciences 2007 - 2010
  • Associate Professor of Chemistry, Chemistry, Trinity College of Arts & Sciences 2002 - 2007
  • Assistant Professor of Chemistry, Chemistry, Trinity College of Arts & Sciences 1995 - 1997
  • Assistant Professor of Biochemistry, Biochemistry, Basic Science Departments 1990 - 1997
• Recognition
• 

  In the News

  • APR 15, 2022

    School of Medicine

    School of Medicine Celebrates 2022 Faculty Achievement Awards
• Expertise
• 

  Subject Headings

  • Arrestins
  • Binding Sites
  • Binding, Competitive
  • Biophysics
  • Calorimetry
  • Circular Dichroism
  • Computer Simulation
  • Deuterium Exchange Measurement
  • Diffusion
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Kinetics
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Models, Chemical
  • Models, Molecular
  • Models, Statistical
  • Models, Theoretical
  • Molecular Conformation
  • Molecular Structure
  • Motion
  • Muser Mentor
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments
  • Pliability
  • Protein Binding
  • Protein Conformation
  • Protein Denaturation
  • Protein Folding
  • Protein Stability
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins
  • RNA, Catalytic
  • Receptors, Adrenergic, beta-2
  • Reproducibility of Results
  • Ribonuclease P
  • Ribonucleases
  • Ribonucleoproteins
  • Spectrometry, Fluorescence
  • Spectrum Analysis
  • Staphylococcal Protein A
  • Structural Homology, Protein
  • Structure-Activity Relationship
  • Temperature
  • Thermodynamics
  • Time Factors
  • Titrimetry
  • Viral Proteins
• Research
• 

  Selected Grants

  • Bioinformatics and Computational Biology Training Program awarded by National Institutes of Health 2005 - 2021
  • Role of protein A structure, folding kinetics and dynamics in S. aureus virulence awarded by National Institutes of Health 2016 - 2021
  • Organization and Function of Cellular Structure awarded by National Institutes of Health 1975 - 2020
  • Structural Biology and Biophysics Training Program awarded by National Institutes of Health 1994 - 2015
  • New Console and Cold Probe for the Duke 600 MHz NMR Spectrometer System awarded by National Institutes of Health 2013 - 2014
  • Mechanistic Studies of Complex Protein Folding Reactions awarded by National Institutes of Health 2008 - 2013
  • NSF MRI Research Triangle X-Ray Scattering Instrumentation: SAXS/WAXS/GISAXS awarded by  National Science Foundation 2012 - 2013
  • Replacement Equipment Components for an 800 MHz NMR Spectrometer awarded by National Institutes of Health 2010 - 2011
  • Purchase of a Q-TOF LC/MS System awarded by National Institutes of Health 2010 - 2011
  • Duke PREP: Minority Recruitment into Biomedical Sciences awarded by National Institutes of Health 2003 - 2008
  • Biophysical Studies of RNase P Protein Folding & Assembly awarded by National Institutes of Health 2001 - 2007
  • RNase P as a Model for Ribonucleoprotein Assembly awarded by National Institutes of Health 2002 - 2005
  • Mechanistic Studies of Protein Folding awarded by National Institutes of Health 1991 - 2005
  • Same awarded by National Institutes of Health 1997 - 2000
  • Nuclear Magnetic Resonance Studies Of Protein Folding awarded by National Institutes of Health 1996 - 1999
  • Molecular Biophysics Training Program awarded by National Institutes of Health 1994 - 1999
  • Structural Studies Of An Hiv-1 Inhibitory Peptide awarded by National Institutes of Health 1993 - 1997
  • Structural Studies Of Bpti Folding Mutants awarded by National Institutes of Health 1991 - 1996
  • Structural Stuides Of An Hiv-1 Inhibitory Peptide awarded by National Institutes of Health 1993 - 1996
  • Structural Studies Of Bpti Folding Mutants awarded by National Institutes of Health 1994 - 1995
  • Structural Studies Of Bpri Folding Mutants awarded by National Institutes of Health 1993 - 1995
  • Circular Dichroism Spectrometer awarded by National Institutes of Health 1993 - 1995
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Gao, Sean, Joanna X. Campbell, Terrence G. Oas, and Katherine J. Franz. “Multiple Modes of Zinc Binding to Histatin 5 Revealed by Buffer-Independent Thermodynamics.” Inorg Chem 62, no. 18 (May 8, 2023): 7087–96. https://doi.org/10.1021/acs.inorgchem.3c00608.
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    • Orlovsky, Nicole I., Hashim M. Al-Hashimi, and Terrence G. Oas. “Exposing Hidden High-Affinity RNA Conformational States.” J Am Chem Soc 142, no. 2 (January 15, 2020): 907–21. https://doi.org/10.1021/jacs.9b10535.
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    • Roberts, Stefan, Tyler S. Harmon, Jeffrey L. Schaal, Vincent Miao, Kan Jonathan Li, Andrew Hunt, Yi Wen, et al. “Injectable tissue integrating networks from recombinant polypeptides with tunable order.” Nat Mater 17, no. 12 (December 2018): 1154–63. https://doi.org/10.1038/s41563-018-0182-6.
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    • Roberts, Stefan, Tyler S. Harmon, Jeffrey L. Schaal, Vincent Miao, Kan Jonathan Li, Andrew Hunt, Yi Wen, et al. “Author Correction: Injectable tissue integrating networks from recombinant polypeptides with tunable order.” Nat Mater 17, no. 12 (December 2018): 1164. https://doi.org/10.1038/s41563-018-0233-z.
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    • Qi, Yang, Jeffrey W. Martin, Adam W. Barb, François Thélot, Anthony K. Yan, Bruce R. Donald, and Terrence G. Oas. “Continuous Interdomain Orientation Distributions Reveal Components of Binding Thermodynamics.” J Mol Biol 430, no. 18 Pt B (September 14, 2018): 3412–26. https://doi.org/10.1016/j.jmb.2018.06.022.
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    • Qi, Yang, Jeffrey Martin, Adam Barb, François Thélot, Anthony Yan, Bruce Donald, and Terrence Oas. “Continuous interdomain orientation distributions reveal components of binding thermodynamics,” October 11, 2017. https://doi.org/10.1101/200238.
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    • Shah, Riddhi, Tomoo Ohashi, Harold P. Erickson, and Terrence G. Oas. “Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.” J Biol Chem 292, no. 3 (January 20, 2017): 955–66. https://doi.org/10.1074/jbc.M116.760371.
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    • Mosley, Pamela L., Kyle G. Daniels, and Terrence G. Oas. “Electrostatic Energetics of Bacillus subtilis Ribonuclease P Protein Determined by Nuclear Magnetic Resonance-Based Histidine pKa Measurements.” Biochemistry 54, no. 35 (September 8, 2015): 5379–88. https://doi.org/10.1021/acs.biochem.5b00138.
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    • Daniels, Kyle G., Yang Suo, and Terrence G. Oas. “Conformational kinetics reveals affinities of protein conformational states.” Proc Natl Acad Sci U S A 112, no. 30 (July 28, 2015): 9352–57. https://doi.org/10.1073/pnas.1502084112.
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    • Deis, Lindsay N., Qinglin Wu, You Wang, Yang Qi, Kyle G. Daniels, Pei Zhou, and Terrence G. Oas. “Suppression of conformational heterogeneity at a protein-protein interface.” Proc Natl Acad Sci U S A 112, no. 29 (July 21, 2015): 9028–33. https://doi.org/10.1073/pnas.1424724112.
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    • Qi, Yang, Jeffrey W. Martin, Anthony Yan, Francois Thelot, Bruce R. Donald, and Terrence G. Oas. “Visualizing the Inter-Domain Motions of a Pathogenic Protein using Sparse RDC Data.” Biophysical Journal 108, no. 2 (January 2015): 58a-58a. https://doi.org/10.1016/j.bpj.2014.11.353.
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    • Deis, Lindsay N., Charles W. Pemble, Yang Qi, Andrew Hagarman, David C. Richardson, Jane S. Richardson, and Terrence G. Oas. “Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity.” Structure 22, no. 10 (October 7, 2014): 1467–77. https://doi.org/10.1016/j.str.2014.08.014.
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    • Capp, Jo A., Andrew Hagarman, David C. Richardson, and Terrence G. Oas. “The statistical conformation of a highly flexible protein: small-angle X-ray scattering of S. aureus protein A.” Structure 22, no. 8 (August 5, 2014): 1184–95. https://doi.org/10.1016/j.str.2014.06.011.
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    • Daniels, Kyle G., Nam K. Tonthat, David R. McClure, Yu-Chu Chang, Xin Liu, Maria A. Schumacher, Carol A. Fierke, Scott C. Schmidler, and Terrence G. Oas. “Ligand concentration regulates the pathways of coupled protein folding and binding.” J Am Chem Soc 136, no. 3 (January 22, 2014): 822–25. https://doi.org/10.1021/ja4086726.
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    • Zhang, Jianming, Zehra Parlak, Carleen M. Bowers, Terrence Oas, and Stefan Zauscher. “Mapping mechanical properties of organic thin films by force-modulation microscopy in aqueous media.” Beilstein J Nanotechnol 3 (2012): 464–74. https://doi.org/10.3762/bjnano.3.53.
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    • Kahsai, Alem W., Kunhong Xiao, Sudarshan Rajagopal, Seungkirl Ahn, Arun K. Shukla, Jinpeng Sun, Terrence G. Oas, and Robert J. Lefkowitz. “Multiple ligand-specific conformations of the β2-adrenergic receptor.” Nat Chem Biol 7, no. 10 (August 21, 2011): 692–700. https://doi.org/10.1038/nchembio.634.
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    • Isom, Daniel G., Philippe R. Marguet, Terrence G. Oas, and Homme W. Hellinga. “A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity.” Proteins 79, no. 4 (April 2011): 1034–47. https://doi.org/10.1002/prot.22932.
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    • Chang, Yu-Chu, William R. Franch, and Terrence G. Oas. “Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance.” Biochemistry 49, no. 44 (November 9, 2010): 9428–37. https://doi.org/10.1021/bi100287y.
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    • Chang, Yu-Chu, and Terrence G. Oas. “Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.” Biochemistry 49, no. 25 (June 29, 2010): 5086–96. https://doi.org/10.1021/bi100222h.
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    • Isom, Daniel G., Eyal Vardy, Terrence G. Oas, and Homme W. Hellinga. “Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity.” Proc Natl Acad Sci U S A 107, no. 11 (March 16, 2010): 4908–13. https://doi.org/10.1073/pnas.0910421107.
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    • Hammes, Gordon G., Yu-Chu Chang, and Terrence G. Oas. “Conformational selection or induced fit: a flux description of reaction mechanism.” Proc Natl Acad Sci U S A 106, no. 33 (August 18, 2009): 13737–41. https://doi.org/10.1073/pnas.0907195106.
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    • Henkels, Christopher H., Yu-Chu Chang, Stacy I. Chamberlin, and Terrence G. Oas. “Dynamics of backbone conformational heterogeneity in Bacillus subtilis ribonuclease P protein.” Biochemistry 46, no. 51 (December 25, 2007): 15062–75. https://doi.org/10.1021/bi701425n.
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    • Schmidler, Scott C., Joseph E. Lucas, and Terrence G. Oas. “Statistical estimation of statistical mechanical models: helix-coil theory and peptide helicity prediction.” J Comput Biol 14, no. 10 (December 2007): 1287–1310. https://doi.org/10.1089/cmb.2007.0008.
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    • Nobles, Kelly N., Ziqiang Guan, Kunhong Xiao, Terrence G. Oas, and Robert J. Lefkowitz. “The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2.” J Biol Chem 282, no. 29 (July 20, 2007): 21370–81. https://doi.org/10.1074/jbc.M611483200.
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    • Valiaev, Alexei, Dong Woo Lim, Terrence G. Oas, Ashutosh Chilkoti, and Stefan Zauscher. “Force-induced prolyl cis-trans isomerization in elastin-like polypeptides.” J Am Chem Soc 129, no. 20 (May 23, 2007): 6491–97. https://doi.org/10.1021/ja070147r.
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    • Chugha, Preeti, and Terrence G. Oas. “Backbone dynamics of the monomeric lambda repressor denatured state ensemble under nondenaturing conditions.” Biochemistry 46, no. 5 (February 6, 2007): 1141–51. https://doi.org/10.1021/bi061371g.
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    • Arora, Pooja, Gordon G. Hammes, and Terrence G. Oas. “Folding mechanism of a multiple independently-folding domain protein: double B domain of protein A.” Biochemistry 45, no. 40 (October 10, 2006): 12312–24. https://doi.org/10.1021/bi060923s.
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    • Henkels, Christopher H., and Terrence G. Oas. “Ligation-state hydrogen exchange: coupled binding and folding equilibria in ribonuclease P protein.” J Am Chem Soc 128, no. 24 (June 21, 2006): 7772–81. https://doi.org/10.1021/ja057279+.
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    • Hilser, Vincent J., Bertrand García-Moreno E, Terrence G. Oas, Greg Kapp, and Steven T. Whitten. “A statistical thermodynamic model of the protein ensemble.” Chem Rev 106, no. 5 (May 2006): 1545–58. https://doi.org/10.1021/cr040423+.
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    • Chugha, Preeti, Harvey J. Sage, and Terrence G. Oas. “Methionine oxidation of monomeric lambda repressor: the denatured state ensemble under nondenaturing conditions.” Protein Sci 15, no. 3 (March 2006): 533–42. https://doi.org/10.1110/ps.051856406.
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    • Henkels, Christopher H., and Terrence G. Oas. “Thermodynamic characterization of the osmolyte- and ligand-folded states of Bacillus subtilis ribonuclease P protein.” Biochemistry 44, no. 39 (October 4, 2005): 13014–26. https://doi.org/10.1021/bi0504613.
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    • Valiaev, A., D. W. Lim, T. Oas, R. L. Clark, A. Chilkoti, and S. Zauscher. “Force-induced proline cis-trans isomerization in elastin-like polypeptides.” Biophysical Journal 88, no. 1 (January 1, 2005): 168A-168A.
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    • Kapp, Gregory T., Jane S. Richardson, and Terrence G. Oas. “Kinetic role of helix caps in protein folding is context-dependent.” Biochemistry 43, no. 13 (April 6, 2004): 3814–23. https://doi.org/10.1021/bi035683k.
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    • Arora, Pooja, Terrence G. Oas, and Jeffrey K. Myers. “Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsec.” Protein Sci 13, no. 4 (April 2004): 847–53. https://doi.org/10.1110/ps.03541304.
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    • Vu, Dung M., Jeffrey K. Myers, Terrence G. Oas, and R Brian Dyer. “Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein.” Biochemistry 43, no. 12 (March 30, 2004): 3582–89. https://doi.org/10.1021/bi036203s.
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    • Dimitriadis, George, Adam Drysdale, Jeffrey K. Myers, Pooja Arora, Sheena E. Radford, Terence G. Oas, and D Alastair Smith. “Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.” Proc Natl Acad Sci U S A 101, no. 11 (March 16, 2004): 3809–14. https://doi.org/10.1073/pnas.0306433101.
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    • Hanson, W Miachel, Scott A. Beeser, Terrence G. Oas, and David P. Goldenberg. “Identification of a residue critical for maintaining the functional conformation of BPTI.” J Mol Biol 333, no. 2 (October 17, 2003): 425–41. https://doi.org/10.1016/j.jmb.2003.08.023.
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    • Powell, Kendall D., Sina Ghaemmaghami, Michael Z. Wang, Liyuan Ma, Terrance G. Oas, and Michael C. Fitzgerald. “A General Mass Spectrometry-Based Assay for the Quantitation of Protein−Ligand Binding Interactions in Solution [J. Am. Chem. Soc. 2002, 124, 10256−10257].” Journal of the American Chemical Society 125, no. 14 (April 1, 2003): 4398–4398. https://doi.org/10.1021/ja0251266.
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    • Fitzgerald, M. C., K. D. Powell, M. Z. Wang, L. Ma, S. Ghaemmaghami, and T. G. Oas. “A general mass spectrometry-based method for the quantitation of protein-ligand binding interactions in solution.” Proceedings 50th Asms Conference on Mass Spectrometry and Allied Topics, December 1, 2002, 395–96.
    • Ghaemmaghami, S., M. C. Fitzgerald, and T. G. Oas. “Quantitative protein stability measurement in living bacteria.” Proceedings 50th Asms Conference on Mass Spectrometry and Allied Topics, December 1, 2002, 109–10.
    • Powell, Kendall D., Sina Ghaemmaghami, Michael Z. Wang, Liyuan Ma, Terrance G. Oas, and Michael C. Fitzgerald. “A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution.” J Am Chem Soc 124, no. 35 (September 4, 2002): 10256–57. https://doi.org/10.1021/ja026574g.
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    • Myers, Jeffrey K., and Terrence G. Oas. “Mechanism of fast protein folding.” Annu Rev Biochem 71 (2002): 783–815. https://doi.org/10.1146/annurev.biochem.71.110601.135346.
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    • Ghaemmaghami, S., and T. G. Oas. “Quantitative protein stability measurement in vivo.” Nat Struct Biol 8, no. 10 (October 2001): 879–82. https://doi.org/10.1038/nsb1001-879.
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    • Myers, J. K., D. P. Morris, A. L. Greenleaf, and T. G. Oas. “Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.” Biochemistry 40, no. 29 (July 24, 2001): 8479–86. https://doi.org/10.1021/bi0027884.
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    • Myers, J. K., and T. G. Oas. “Preorganized secondary structure as an important determinant of fast protein folding.” Nat Struct Biol 8, no. 6 (June 2001): 552–58. https://doi.org/10.1038/88626.
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    • Henkels, C. H., J. C. Kurz, C. A. Fierke, and T. G. Oas. “Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein.” Biochemistry 40, no. 9 (March 6, 2001): 2777–89. https://doi.org/10.1021/bi002078y.
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    • Ghaemmaghami, S., M. C. Fitzgerald, and T. G. Oas. “A quantitative, high-throughput screen for protein stability.” Proc Natl Acad Sci U S A 97, no. 15 (July 18, 2000): 8296–8301. https://doi.org/10.1073/pnas.140111397.
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    • Burton, R. E., J. A. Hunt, C. A. Fierke, and T. G. Oas. “Novel disulfide engineering in human carbonic anhydrase II using the PAIRWISE side-chain geometry database.” Protein Sci 9, no. 4 (April 2000): 776–85. https://doi.org/10.1110/ps.9.4.776.
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    • Oas, T. G. “Mechanism of folding fast: Experimental and theoretical studies of monomeric lambda repressor.” Abstracts of Papers of the American Chemical Society 219 (March 26, 2000): U283–U283.
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    • Myers, J. K., and T. G. Oas. “Reinterpretation of GCN4-p1 folding kinetics: partial helix formation precedes dimerization in coiled coil folding.” J Mol Biol 289, no. 2 (June 4, 1999): 205–9. https://doi.org/10.1006/jmbi.1999.2747.
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    • Myers, J. K., and T. G. Oas. “Contribution of a buried hydrogen bond to lambda repressor folding kinetics.” Biochemistry 38, no. 21 (May 25, 1999): 6761–68. https://doi.org/10.1021/bi990088x.
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    • Beeser, S. A., T. G. Oas, and D. P. Goldenberg. “Determinants of backbone dynamics in native BPTI: cooperative influence of the 14-38 disulfide and the Tyr35 side-chain.” J Mol Biol 284, no. 5 (December 18, 1998): 1581–96. https://doi.org/10.1006/jmbi.1998.2240.
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    • Hilser, V. J., D. Dowdy, T. G. Oas, and E. Freire. “The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble.” Proc Natl Acad Sci U S A 95, no. 17 (August 18, 1998): 9903–8. https://doi.org/10.1073/pnas.95.17.9903.
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    • Ghaemmaghami, S., J. M. Word, R. E. Burton, J. S. Richardson, and T. G. Oas. “Folding kinetics of a fluorescent variant of monomeric lambda repressor.” Biochemistry 37, no. 25 (June 23, 1998): 9179–85. https://doi.org/10.1021/bi980356b.
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    • Burton, R. E., J. K. Myers, and T. G. Oas. “Protein folding dynamics: quantitative comparison between theory and experiment.” Biochemistry 37, no. 16 (April 21, 1998): 5337–43. https://doi.org/10.1021/bi980245c.
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    • Burton, R. S., J. K. Myers, and T. G. Oas. “Ultrafast folding of monomeric lambda repressor: Experimental characterization and accurate theoretical prediction of folding rates.” Biophysical Journal 74, no. 2 (February 1, 1998): A24–A24.
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    • Burton, R. E., R. S. Busby, and T. G. Oas. “ALASKA: A Mathematica package for two-state kinetic analysis of protein folding reactions.” Journal of Biomolecular Nmr 11, no. 3 (January 1, 1998): 355–60. https://doi.org/10.1023/a:1008276703114.
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    • Beeser, S. A., D. P. Goldenberg, and T. G. Oas. “Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI.” J Mol Biol 269, no. 1 (May 30, 1997): 154–64. https://doi.org/10.1006/jmbi.1997.1031.
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    • Burton, R. E., G. S. Huang, M. A. Daugherty, T. L. Calderone, and T. G. Oas. “The energy landscape of a fast-folding protein mapped by Ala-->Gly substitutions.” Nat Struct Biol 4, no. 4 (April 1997): 305–10. https://doi.org/10.1038/nsb0497-305.
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    • Burton, R. E., G. S. Huang, M. A. Daugherty, P. W. Fullbright, and T. G. Oas. “Microsecond protein folding through a compact transition state.” J Mol Biol 263, no. 2 (October 25, 1996): 311–22. https://doi.org/10.1006/jmbi.1996.0577.
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    • Calderone, T. L., R. D. Stevens, and T. G. Oas. “High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli.” J Mol Biol 262, no. 4 (October 4, 1996): 407–12. https://doi.org/10.1006/jmbi.1996.0524.
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    • Huang, G. S., and T. G. Oas. “Heat and cold denatured states of monomeric lambda repressor are thermodynamically and conformationally equivalent.” Biochemistry 35, no. 20 (May 21, 1996): 6173–80. https://doi.org/10.1021/bi960250l.
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    • Huang, G. S., and T. G. Oas. “Heat and cold denatured states of monomeric λ represser are thermodynamically and conformationally equivalen.” Biochemistry 35, no. 20 (May 21, 1996).
    • Huang, G. S., and T. G. Oas. “Submillisecond folding of monomeric lambda repressor.” Proc Natl Acad Sci U S A 92, no. 15 (July 18, 1995): 6878–82. https://doi.org/10.1073/pnas.92.15.6878.
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    • Huang, G. S., and T. G. Oas. “Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding.” Biochemistry 34, no. 12 (March 28, 1995): 3884–92. https://doi.org/10.1021/bi00012a003.
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    • Breiner, K. M., H. H. Thorp, M. A. Daugherty, and T. G. Oas. “An Anionic Diplatinum DNA Photocleavage Agent: Chemical Mechanism and Footprinting of λ Repressor.” Journal of the American Chemical Society 117, no. 47 (January 1, 1995): 11673–79. https://doi.org/10.1021/ja00152a007.
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    • Wild, C., J. W. Dubay, T. Greenwell, T. Baird, T. G. Oas, C. McDanal, E. Hunter, and T. Matthews. “Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex.” Proc Natl Acad Sci U S A 91, no. 26 (December 20, 1994): 12676–80. https://doi.org/10.1073/pnas.91.26.12676.
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    • Oas, T. G., and S. A. Endow. “Springs and hinges: dynamic coiled coils and discontinuities.” Trends Biochem Sci 19, no. 2 (February 1994): 51–54. https://doi.org/10.1016/0968-0004(94)90030-2.
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    • Wild, C., T. Oas, C. McDanal, D. Bolognesi, and T. Matthews. “A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition.” Proc Natl Acad Sci U S A 89, no. 21 (November 1, 1992): 10537–41. https://doi.org/10.1073/pnas.89.21.10537.
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    • CHERVENAK, M. C., T. G. OAS, and E. J. TOONE. “STRUCTURE AND ENERGETICS OF CONCANAVALIN A-OLIGOSACCHARIDE BINDING.” Abstracts of Papers of the American Chemical Society 204 (August 23, 1992): 102-CARB.
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    • Copié, V., A. C. Kolbert, D. H. Drewry, P. A. Bartlett, T. G. Oas, and R. G. Griffin. “Inhibition of thermolysin by phosphonamidate transition-state analogues: measurement of 31P-15N bond lengths and chemical shifts in two enzyme-inhibitor complexes by solid-state nuclear magnetic resonance.” Biochemistry 29, no. 39 (October 2, 1990): 9176–84. https://doi.org/10.1021/bi00491a011.
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    • Oas, T. G., L. P. McIntosh, E. K. O’Shea, F. W. Dahlquist, and P. S. Kim. “Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy.” Biochemistry 29, no. 12 (March 27, 1990): 2891–94. https://doi.org/10.1021/bi00464a001.
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    • OAS, T. G., J. P. STALEY, D. Y. KWON, E. M. GOODMAN, R. RUKOWSKI, and P. S. KIM. “PEPTIDE MODELS AND THE FOLDING OF BPTI.” Biophysical Journal 57, no. 2 (February 1, 1990): A3–A3.
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    • Myers, R. A., J. M. Mcintosh, J. Imperial, R. W. Williams, T. Oas, J. A. Haack, J. F. Hernandez, J. Rivier, L. J. Cruz, and B. M. Olivera. “Peptides from conus venoms which affect ca^+plus; entry into neurons.” Toxin Reviews 9, no. 2 (January 1, 1990): 179–202. https://doi.org/10.3109/15569549009033113.
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    • Oas, T. G., C. J. Hartzell, G. P. Drobny, and F. W. Dahlquist. “Selective NMR detection of ¹³C¹⁵N dipole pairs in solid samples.” Journal of Magnetic Resonance (1969) 81, no. 2 (February 1, 1989): 395–99. https://doi.org/10.1016/0022-2364(89)90072-3.
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    • Kolbert, A. C., H. J. M. De Groot, T. G. Oas, and R. G. Griffin. “Two-Dimensional Hybrid Experiments for the Measurement of Small Anisotropies in Magic-Angle Spinning Nuclear Magnetic Resonance” 13, no. C (January 1, 1989): 183–94. https://doi.org/10.1016/B978-0-12-025513-9.50013-6.
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    • Raleigh, D. P., A. C. Kolbert, T. G. Oas, M. H. Levitt, and R. G. Griffin. “Enhancement of the effect of small anisotropies in magic-angle spinning nuclear magnetic resonance.” Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases 84, no. 11 (December 1, 1988): 3691–3711. https://doi.org/10.1039/F19888403691.
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    • Oas, T. G., and P. S. Kim. “A peptide model of a protein folding intermediate.” Nature 336, no. 6194 (November 3, 1988): 42–48. https://doi.org/10.1038/336042a0.
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    • Levitt, M. H., T. G. Oas, and R. G. Griffin. “Rotary Resonance Recoupling in Heteronuclear Spin Pair Systems.” Israel Journal of Chemistry 28, no. 4 (January 1, 1988): 271–82. https://doi.org/10.1002/ijch.198800039.
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    • Oas, T. G., G. P. Drobny, and F. W. Dahlquistt. “A new iterative least-squares method for the extraction of NMR parameters from nonideal powder patterns.” Journal of Magnetic Resonance (1969) 78, no. 3 (January 1, 1988): 408–24. https://doi.org/10.1016/0022-2364(88)90129-1.
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    • Oas, T. G., R. G. Griffin, and M. H. Levitt. “Rotary resonance recoupling of dipolar interactions in solid-state nuclear magnetic resonance spectroscopy.” The Journal of Chemical Physics 89, no. 2 (January 1, 1988): 692–95. https://doi.org/10.1063/1.455191.
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    • Hartzell, C. J., M. Whitfield, T. G. Oas, and G. P. Drobny. “Determination of the ¹⁵N and ¹³C Chemical Shift Tensors of L-[¹³C]Alanyl-L-[¹⁵N]alanine from the Dipole-Coupled Powder Patterns.” Journal of the American Chemical Society 109, no. 20 (September 1, 1987): 5966–69. https://doi.org/10.1021/ja00254a012.
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    • Oas, T. G., C. J. Hartzell, T. J. Mcmahon, G. P. Drobny, and F. W. Dahlauist. “The Carbonyl ¹³C Chemical Shift Tensors of Five Peptides Determined from ¹⁵N Dipole-Coupled Chemical Shift Powder Patterns.” Journal of the American Chemical Society 109, no. 20 (September 1, 1987): 5956–62. https://doi.org/10.1021/ja00254a010.
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    • Oas, T. G., C. J. Hartzell, F. W. Dahlquist, and G. P. Drobny. “The Amide ¹⁵N Chemical Shift Tensors of Four Peptides Determined from ¹³C Dipole-Coupled Chemical Shift Powder Patterns.” Journal of the American Chemical Society 109, no. 20 (September 1, 1987): 5962–66. https://doi.org/10.1021/ja00254a011.
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    • OAS, T. G., C. J. HARTZELL, F. W. DAHLQUIST, and G. P. DROBNY. “A NEW APPROACH TO LEAST-SQUARES FITTING ANALYSIS OF NMR POWDER PATTERNS.” Biophysical Journal 51, no. 2 (February 1, 1987): A80–A80.
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    • Hartzell, C. J., M. Whitfield, T. G. Oas, and G. P. Drobny. “Determination of the ¹⁵N and ¹³C chemical shift tensors of L-[¹³C]alanyl-L-[¹⁵N]alanine from the dipole-coupled powder patterns.” Journal of the American Chemical Society 109, no. 20 (1987): 5966–69.
    • OAS, T. G., C. J. HARTZELL, F. W. DAHLQUIST, and G. DROBNY. “N-15 AMIDE CHEMICAL-SHIFT TENSORS OF SEVERAL DIPEPTIDES.” Biophysical Journal 49, no. 2 (February 1, 1986): A328–A328.
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    • Griffey, R. H., A. G. Redfield, L. P. McIntosh, T. G. Oas, and F. W. Dahlquist. “Assignment of Proton Amide Resonances of T4 Lysozyme by ¹³C and ¹⁵N Multiple Isotopic Labeling.” Journal of the American Chemical Society 108, no. 21 (January 1, 1986): 6816–17. https://doi.org/10.1021/ja00281a066.
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    • OAS, T. G., T. J. MCMAHON, F. W. DAHLQUIST, and G. DROBNY. “C-13 CARBONYL CHEMICAL-SHIFT TENSORS OF 3 GLYCINE DIPEPTIDES.” Biophysical Journal 47, no. 2 (January 1, 1985): A331–A331.
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    • Meyers1, P. A., and T. G. Oas. “Comparison of Associations of Different Hydrocarbons with Clay Particles in Simulated Seawater.” Environmental Science and Technology 12, no. 8 (January 1, 1978): 934–37. https://doi.org/10.1021/es60144a005.
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  • Conference Papers

    • Li, Kan, Roy Hughes, and Terrence G. Oas. “Developing Quantitative NMR Methods For Predicting Residue Specific Helicity Of MetO-lambda Unfolded State.” In Protein Science, 23:265–66. WILEY-BLACKWELL, 2014.
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    • Qi, Yang, Jeffrey W. Martin, Bruce R. Donald, and Terrence G. Oas. “Visualizing the Inter-domain Motions of a Flexible Protein Using Continuous Models.” In Protein Science, 23:113–14. WILEY-BLACKWELL, 2014.
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    • Shah, Riddhi S., Terrence G. Oas, and Harold P. Erickson. “Determining the Rate of Unfolding and Refolding of FNIII Domains by Labeling Buried Cysteine.” In Biophysical Journal, 106:289A-289A. CELL PRESS, 2014.
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    • Oas, Terrence G. “PHYS 26-When folding is coupled to binding: How do we tell which comes first?” In Abstracts of Papers of the American Chemical Society, Vol. 236. AMER CHEMICAL SOC, 2008.
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    • Nobles, K. N., Z. Q. Guan, K. H. Xiao, T. G. Oas, and R. J. Lefkowitz. “Conformational changes in beta-arrestin1: The importance of beta-arrestin1's N-domain.” In Faseb Journal, 20:A114–A114. FEDERATION AMER SOC EXP BIOL, 2006.
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    • Xiao, K. H., S. K. Shenoy, K. Nobles, T. G. Oas, and R. J. Lefkowitz. “Activation dependent conformational changes in beta-arrestin 2.” In Biophysical Journal, 88:554A-554A. BIOPHYSICAL SOCIETY, 2005.
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    • Vu, D. M., J. K. Myers, T. G. Oas, and R. B. Dyer. “Fast events in protein folding: Relaxation dynamics of a small three-helix bundle protein.” In Biophysical Journal, 84:166A-166A. BIOPHYSICAL SOCIETY, 2003.
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    • WILD, C., T. BAIRD, C. MCDANAL, T. GREENWELL, T. OAS, and T. MATTHEWS. “ANTIVIRAL ACTIVITY AND MECHANISM OF INHIBITION OF GP41 DERIVED SYNTHETIC PEPTIDES.” In Aids Research and Human Retroviruses, 10:S33–S33. MARY ANN LIEBERT INC PUBL, 1994.
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    • WILD, C., T. OAS, C. MCDANAL, D. BOLOGNESI, and T. MATTHEWS. “A PEPTIDE INHIBITOR OF HIV-1 REPLICATION - CORRELATION BETWEEN SOLUTION STRUCTURE AND VIRAL INHIBITION.” In Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology, 6:675–675. LIPPINCOTT-RAVEN PUBL, 1993.
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    • WILD, C., T. OAS, C. MCDANAL, D. BOLOGNESI, and T. MATTHEWS. “A SYNTHETIC PEPTIDE INHIBITOR OF HUMAN-IMMUNODEFICIENCY-VIRUS REPLICATION - CORRELATION BETWEEN SOLUTION STRUCTURE AND VIRAL INHIBITION.” In Journal of Cellular Biochemistry, 222–222. WILEY-LISS, 1993.
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    • COPIE, V., A. KOLBERT, D. DREWRY, P. BARTLETT, T. OAS, and R. GRIFFIN. “STRUCTURAL STUDIES OF THERMOLYSIN-INHIBITOR COMPLEXES WITH SOLID-STATE NMR - MEASUREMENTS OF P-31-N-15 BOND LENGTHS AND CHEMICAL-SHIFTS.” In Biophysical Journal, 57:A40–A40. BIOPHYSICAL SOCIETY, 1990.
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    • OAS, T. G., and P. S. KIM. “A PROTEIN FOLDING INTERMEDIATE ANALOG - DESIGN, SYNTHESIS, AND CHARACTERIZATION.” In Protein Folding : Deciphering the Second Half of the Genetic Code, edited by L. M. GIERASCH and J. KING, 123–28. AMER ASSOC ADVANCEMENT SCIENCE, 1990.
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    • KOLBERT, A. C., H. J. M. DEGROOT, T. G. OAS, and R. G. GRIFFIN. “2-DIMENSIONAL HYBRID EXPERIMENTS FOR THE MEASUREMENT OF SMALL ANISOTROPIES IN MAGIC-ANGLE SPINNING NUCLEAR-MAGNETIC-RESONANCE.” In Advances in Magnetic Resonance, Vol 13, edited by W. S. WARREN, 13:183–94. ACADEMIC PRESS INC, 1989.
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    • MAYNE, L., T. RAMAHI, T. OAS, and B. HUDSON. “ULTRAVIOLET RESONANCE RAMAN STUDIES OF PEPTIDE COMPONENTS.” In Biophysical Journal, 45:A322–A322. BIOPHYSICAL SOCIETY, 1984.
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• Teaching & Mentoring
• 

  Recent Courses

  • BIOCHEM 302: Introductory Biochemistry II 2023
  • BIOCHEM 393: Research Independent Study 2023
  • BIOCHEM 593: Research Independent Study 2023
  • BIOCHEM 681: Biophysical Methods 2023
  • CMB 710F: Cell & Molecular Biology Module VI 2023
  • BIOCHEM 302: Introductory Biochemistry II 2022
  • BIOCHEM 393: Research Independent Study 2022
  • BIOCHEM 593: Research Independent Study 2022
  • BIOCHEM 681: Biophysical Methods 2022
  • CMB 710F: Cell & Molecular Biology Module VI 2022
  • BIOCHEM 393: Research Independent Study 2021
  • BIOCHEM 593: Research Independent Study 2021
  • BIOCHEM 681: Biophysical Methods 2021
  • CMB 710E: Cell & Molecular Biology Module V 2021

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