Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • Ph.D., University of Cambridge (United Kingdom) 1986
• 

  Previous Appointments & Affiliations

  • Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 2015
  • Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 2015
  • Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 1992 - 2014
  • Professor of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 2005 - 2008
  • Associate Professor of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 1999 - 2005
  • Associate Professor of Biochemistry with Tenure, Biochemistry, Basic Science Departments 1999 - 2004
  • Assistant Professor of Biochemistry, Biochemistry, Basic Science Departments 1992 - 1999
  • Assistant Professor of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 1994 - 1999
• Recognition
• 

  Awards & Honors

  • Emil Thomas Kaiser Award. Protein Society,The. 2004
• Research
• 

  Selected Grants

  • Structure and Mechanism of Protein Prenyltransferases awarded by National Institutes of Health 1995 - 2016
  • Structural biology of human DNA mismatch repair machinery awarded by National Institutes of Health 2009 - 2012
  • NIH Director's Pioneer Award awarded by National Institutes of Health 2004 - 2010
  • Biological Oscilloscopes: Spatio-Temporal Metabolomics awarded by National Institutes of Health 2004 - 2008
  • Structure-based Design of Protein Function awarded by National Institutes of Health 1994 - 2008
  • Computational enzyme design awarded by National Institutes of Health 2005 - 2007
  • Computational Redesign of Nuclear Hormone Receptors awarded by National Institutes of Health 2004 - 2006
  • Computational Geometry for Structural Biology and Bioinformatics awarded by  National Science Foundation 2000 - 2005
  • Time-resolved fluorescents spectroscopy instrumentation for analysis of engineered biosensor proteins awarded by Office of Naval Research 2004 - 2005
  • Zeiss LSM510 META confocal-fluorescence spectroscopy awarded by National Institutes of Health 2003 - 2004
  • Development of Novel Biosensors for Detecting TNT and Its Decomposition Products in Seawater awarded by Office of Naval Research 2001 - 2004
  • Hign-throughput screening robotics for directed evolution of engineered sensor proteins awarded by Office of Naval Research 2002 - 2003
  • Instrumentation for the Interfacial Analysis of Biosensor Microsystems Containing Genetically Engineered Receptor Protei awarded by Office of Naval Research 2001 - 2002
  • Systematic Isolation Of New Biosensors By Protein Engineer awarded by Office of Naval Research 1997 - 2001
  • Study Of Binuclear Copper Centers By Protein Design awarded by National Institutes of Health 1999 - 2000
  • Same awarded by Office of Naval Research 1999 - 2000
  • same awarded by Office of Naval Research 1998 - 1999
  • Constructiion Of New Metalloproteins By Rational Design awarded by National Institutes of Health 1994 - 1999
  • Construction Of New Metalloproteins By Rational Design awarded by National Institutes of Health 1994 - 1999
  • Construction Of New Metalloproteins By Rational Design awarded by National Institutes of Health 1994 - 1999
  • Construction Of New Metalloproteins By Rational Design awarded by National Institutes of Health 1994 - 1999
  • Construction Of Newe Metalloproteins By Rational Design awarded by National Institutes of Health 1994 - 1999
• 

  External Relationships

  • Precision Bioscience
  • Protabit
  • SenGenix
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Wang, You, Feng Xu, Connie B. Nichols, Yuqian Shi, Homme W. Hellinga, J Andrew Alspaugh, Mark D. Distefano, and Lorena S. Beese. “Structure-Guided Discovery of Potent Antifungals that Prevent Ras Signaling by Inhibiting Protein Farnesyltransferase.” J Med Chem 65, no. 20 (October 27, 2022): 13753–70. https://doi.org/10.1021/acs.jmedchem.2c00902.
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    • Allert, Malin J., and Homme W. Hellinga. “Discovery of Thermostable, Fluorescently Responsive Glucose Biosensors by Structure-Assisted Function Extrapolation.” Biochemistry 61, no. 4 (February 15, 2022): 276–93. https://doi.org/10.1021/acs.biochem.1c00738.
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    • Allert, Malin J., and Homme W. Hellinga. “Harnessing Environmental Ca2+ for Extracellular Protein Thermostabilization.” Biochemistry 59, no. 39 (October 6, 2020): 3725–40. https://doi.org/10.1021/acs.biochem.0c00449.
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    • Allert, Malin J., and Homme W. Hellinga. “Describing Complex Structure-Function Relationships in Biomolecules at Equilibrium.” J Mol Biol 432, no. 7 (March 27, 2020): 1926–51. https://doi.org/10.1016/j.jmb.2019.12.039.
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    • Shi, Yuqian, Homme W. Hellinga, and Lorena S. Beese. “Interplay of catalysis, fidelity, threading, and processivity in the exo- and endonucleolytic reactions of human exonuclease I.” Proc Natl Acad Sci U S A 114, no. 23 (June 6, 2017): 6010–15. https://doi.org/10.1073/pnas.1704845114.
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    • Mabanglo, Mark F., Michael A. Hast, Nathan B. Lubock, Homme W. Hellinga, and Lorena S. Beese. “Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.” Protein Sci 23, no. 3 (March 2014): 289–301. https://doi.org/10.1002/pro.2411.
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    • Grimley, Joshua S., Li Li, Weina Wang, Lei Wen, Lorena S. Beese, Homme W. Hellinga, and George J. Augustine. “Visualization of synaptic inhibition with an optogenetic sensor developed by cell-free protein engineering automation.” J Neurosci 33, no. 41 (October 9, 2013): 16297–309. https://doi.org/10.1523/JNEUROSCI.4616-11.2013.
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    • Wang, Weina, Eugene Y. Wu, Homme W. Hellinga, and Lorena S. Beese. “Structural factors that determine selectivity of a high fidelity DNA polymerase for deoxy-, dideoxy-, and ribonucleotides.” J Biol Chem 287, no. 34 (August 17, 2012): 28215–26. https://doi.org/10.1074/jbc.M112.366609.
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    • Wang, Weina, Homme W. Hellinga, and Lorena S. Beese. “Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis.” Proc Natl Acad Sci U S A 108, no. 43 (October 25, 2011): 17644–48. https://doi.org/10.1073/pnas.1114496108.
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    • Hast, Michael A., Connie B. Nichols, Stephanie M. Armstrong, Shannon M. Kelly, Homme W. Hellinga, J Andrew Alspaugh, and Lorena S. Beese. “Structures of Cryptococcus neoformans protein farnesyltransferase reveal strategies for developing inhibitors that target fungal pathogens.” J Biol Chem 286, no. 40 (October 7, 2011): 35149–62. https://doi.org/10.1074/jbc.M111.250506.
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    • Layton, Curtis J., and Homme W. Hellinga. “Quantitation of protein-protein interactions by thermal stability shift analysis.” Protein Sci 20, no. 8 (August 2011): 1439–50. https://doi.org/10.1002/pro.674.
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    • Layton, Curtis J., and Homme W. Hellinga. “Integration of cell-free protein coexpression with an enzyme-linked immunosorbent assay enables rapid analysis of protein-protein interactions directly from DNA.” Protein Sci 20, no. 8 (August 2011): 1432–38. https://doi.org/10.1002/pro.675.
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    • Orans, Jillian, Elizabeth A. McSweeney, Ravi R. Iyer, Michael A. Hast, Homme W. Hellinga, Paul Modrich, and Lorena S. Beese. “Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family.” Cell 145, no. 2 (April 15, 2011): 212–23. https://doi.org/10.1016/j.cell.2011.03.005.
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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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    • Antunes, Mauricio S., Kevin J. Morey, J Jeff Smith, Kirk D. Albrecht, Tessa A. Bowen, Jeffrey K. Zdunek, Jared F. Troupe, et al. “Programmable ligand detection system in plants through a synthetic signal transduction pathway.” Plos One 6, no. 1 (January 25, 2011): e16292. https://doi.org/10.1371/journal.pone.0016292.
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    • Layton, Curtis J., and Homme W. Hellinga. “Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-throughput determination of ligand affinities with extrinsic fluorescent dyes.” Biochemistry 49, no. 51 (December 28, 2010): 10831–41. https://doi.org/10.1021/bi101414z.
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    • Allert, Malin, J Colin Cox, and Homme W. Hellinga. “Multifactorial determinants of protein expression in prokaryotic open reading frames.” J Mol Biol 402, no. 5 (October 8, 2010): 905–18. https://doi.org/10.1016/j.jmb.2010.08.010.
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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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    • Cuneo, Matthew J., Lorena S. Beese, and Homme W. Hellinga. “Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold.” J Biol Chem 284, no. 48 (November 27, 2009): 33217–23. https://doi.org/10.1074/jbc.M109.041624.
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    • Cuneo, Matthew J., Anita Changela, Lorena S. Beese, and Homme W. Hellinga. “Structural adaptations that modulate monosaccharide, disaccharide, and trisaccharide specificities in periplasmic maltose-binding proteins.” J Mol Biol 389, no. 1 (May 29, 2009): 157–66. https://doi.org/10.1016/j.jmb.2009.04.008.
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    • Antunes, Mauricio S., Kevin J. Morey, Neera Tewari-Singh, Tessa A. Bowen, J Jeff Smith, Colleen T. Webb, Homme W. Hellinga, and June I. Medford. “Engineering key components in a synthetic eukaryotic signal transduction pathway.” Mol Syst Biol 5 (2009): 270. https://doi.org/10.1038/msb.2009.28.
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    • Cuneo, Matthew J., Anita Changela, Aleksandr E. Miklos, Lorena S. Beese, Joanna K. Krueger, and Homme W. Hellinga. “Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport.” J Biol Chem 283, no. 47 (November 21, 2008): 32812–20. https://doi.org/10.1074/jbc.M803595200.
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    • Cuneo, Matthew J., Lorena S. Beese, and Homme W. Hellinga. “Ligand-induced conformational changes in a thermophilic ribose-binding protein.” Bmc Struct Biol 8 (November 19, 2008): 50. https://doi.org/10.1186/1472-6807-8-50.
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    • Smith, Adam J. T., Roger Müller, Miguel D. Toscano, Peter Kast, Homme W. Hellinga, Donald Hilvert, and K. N. Houk. “Structural reorganization and preorganization in enzyme active sites: comparisons of experimental and theoretically ideal active site geometries in the multistep serine esterase reaction cycle.” J Am Chem Soc 130, no. 46 (November 19, 2008): 15361–73. https://doi.org/10.1021/ja803213p.
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    • Hellinga, Homme W. “In the wake of two retractions, a request for investigation.” Nature 454, no. 7203 (July 24, 2008): 397. https://doi.org/10.1038/454397b.
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    • Cuneo, Matthew J., Yaji Tian, Malin Allert, and Homme W. Hellinga. “The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homolog.” Bmc Struct Biol 8 (March 28, 2008): 20. https://doi.org/10.1186/1472-6807-8-20.
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    • Dwyer, Mary A., Loren L. Looger, and Homme W. Hellinga. “Retraction.” Science 319, no. 5863 (February 1, 2008): 569. https://doi.org/10.1126/science.319.5863.569b.
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    • Tian, Yaji, Matthew J. Cuneo, Anita Changela, Birte Höcker, Lorena S. Beese, and Homme W. Hellinga. “Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein.” Protein Sci 16, no. 10 (October 2007): 2240–50. https://doi.org/10.1110/ps.072969407.
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    • Cox, J Colin, Janel Lape, Mahmood A. Sayed, and Homme W. Hellinga. “Protein fabrication automation.” Protein Sci 16, no. 3 (March 2007): 379–90. https://doi.org/10.1110/ps.062591607.
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    • Allert, Malin, Mary A. Dwyer, and Homme W. Hellinga. “Local encoding of computationally designed enzyme activity.” J Mol Biol 366, no. 3 (February 23, 2007): 945–53. https://doi.org/10.1016/j.jmb.2006.12.002.
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    • Cuneo, Matthew J., Anita Changela, Joshua J. Warren, Lorena S. Beese, and Homme W. Hellinga. “The crystal structure of a thermophilic glucose binding protein reveals adaptations that interconvert mono and di-saccharide binding sites.” J Mol Biol 362, no. 2 (September 15, 2006): 259–70. https://doi.org/10.1016/j.jmb.2006.06.084.
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    • Lorimier, Robert M. de, Yaji Tian, and Homme W. Hellinga. “Binding and signaling of surface-immobilized reagentless fluorescent biosensors derived from periplasmic binding proteins.” Protein Sci 15, no. 8 (August 2006): 1936–44. https://doi.org/10.1110/ps.062261606.
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    • Rizk, Shahir S., Matthew J. Cuneo, and Homme W. Hellinga. “Identification of cognate ligands for the Escherichia coli phnD protein product and engineering of a reagentless fluorescent biosensor for phosphonates.” Protein Sci 15, no. 7 (July 2006): 1745–51. https://doi.org/10.1110/ps.062135206.
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    • Yang, Wei, Anna L. Wilkins, Yiming Ye, Zhi-ren Liu, Shun-yi Li, Jeffrey L. Urbauer, Homme W. Hellinga, Alice Kearney, P Anton van der Merwe, and Jenny J. Yang. “Design of a calcium-binding protein with desired structure in a cell adhesion molecule.” J Am Chem Soc 127, no. 7 (February 23, 2005): 2085–93. https://doi.org/10.1021/ja0431307.
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    • Dattelbaum, Jonathan D., Loren L. Looger, David E. Benson, Kevin M. Sali, Richard B. Thompson, and Homme W. Hellinga. “Analysis of allosteric signal transduction mechanisms in an engineered fluorescent maltose biosensor.” Protein Sci 14, no. 2 (February 2005): 284–91. https://doi.org/10.1110/ps.041146005.
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    • Smith, J Jefferson, David W. Conrad, Matthew J. Cuneo, and Homme W. Hellinga. “Orthogonal site-specific protein modification by engineering reversible thiol protection mechanisms.” Protein Sci 14, no. 1 (January 2005): 64–73. https://doi.org/10.1110/ps.04965405.
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    • Dwyer, Mary A., and Homme W. Hellinga. “Periplasmic binding proteins: a versatile superfamily for protein engineering.” Curr Opin Struct Biol 14, no. 4 (August 2004): 495–504. https://doi.org/10.1016/j.sbi.2004.07.004.
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    • Hellinga, H. “Protein constructed to detect nerve agent weapons.” Industrial Bioprocessing 26, no. 7 (July 1, 2004): 6–7.
    • Dwyer, Mary A., Loren L. Looger, and Homme W. Hellinga. “Computational design of a biologically active enzyme.” Science 304, no. 5679 (June 25, 2004): 1967–71. https://doi.org/10.1126/science.1098432.
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    • Allert, Malin, Shahir S. Rizk, Loren L. Looger, and Homme W. Hellinga. “Computational design of receptors for an organophosphate surrogate of the nerve agent soman.” Proc Natl Acad Sci U S A 101, no. 21 (May 25, 2004): 7907–12. https://doi.org/10.1073/pnas.0401309101.
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    • Dwyer, M. A., L. L. Looger, and H. W. Hellinga. “Computational design of a Zn2+ receptor that controls bacterial gene expression.” Proc Natl Acad Sci U S A 100, no. 20 (September 30, 2003): 11255–60. https://doi.org/10.1073/pnas.2032284100.
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    • Yang, Wei, Lisa M. Jones, Leanne Isley, Yiming Ye, Hsiau-Wei Lee, Anna Wilkins, Zhi-ren Liu, et al. “Rational design of a calcium-binding protein.” J Am Chem Soc 125, no. 20 (May 21, 2003): 6165–71. https://doi.org/10.1021/ja034724x.
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    • Wisz, Michael S., and Homme W. Hellinga. “An empirical model for electrostatic interactions in proteins incorporating multiple geometry-dependent dielectric constants.” Proteins 51, no. 3 (May 15, 2003): 360–77. https://doi.org/10.1002/prot.10332.
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    • Looger, Loren L., Mary A. Dwyer, James J. Smith, and Homme W. Hellinga. “Computational design of receptor and sensor proteins with novel functions.” Nature 423, no. 6936 (May 8, 2003): 185–90. https://doi.org/10.1038/nature01556.
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    • Liu, Haiqing, Jacob J. Schmidt, George D. Bachand, Shahir S. Rizk, Loren L. Looger, Homme W. Hellinga, and Carlo D. Montemagno. “Control of a biomolecular motor-powered nanodevice with an engineered chemical switch.” Nat Mater 1, no. 3 (November 2002): 173–77. https://doi.org/10.1038/nmat761.
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    • Lorimier, Robert M. de, J Jeff Smith, Mary A. Dwyer, Loren L. Looger, Kevin M. Sali, Chad D. Paavola, Shahir S. Rizk, et al. “Construction of a fluorescent biosensor family.” Protein Sci 11, no. 11 (November 2002): 2655–75. https://doi.org/10.1110/ps.021860.
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    • Yang, Wei, Hsiau-Wei Lee, Homme Hellinga, and Jenny J. Yang. “Structural analysis, identification, and design of calcium-binding sites in proteins.” Proteins 47, no. 3 (May 15, 2002): 344–56. https://doi.org/10.1002/prot.10093.
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    • Benson, David E., Alice E. Haddy, and Homme W. Hellinga. “Converting a maltose receptor into a nascent binuclear copper oxygenase by computational design.” Biochemistry 41, no. 9 (March 5, 2002): 3262–69. https://doi.org/10.1021/bi011359i.
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    • Long, S. B., P. J. Hancock, A. M. Kral, H. W. Hellinga, and L. S. Beese. “The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.” Proc Natl Acad Sci U S A 98, no. 23 (November 6, 2001): 12948–53. https://doi.org/10.1073/pnas.241407898.
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    • Marvin, J. S., and H. W. Hellinga. “Manipulation of ligand binding affinity by exploitation of conformational coupling.” Nat Struct Biol 8, no. 9 (September 2001): 795–98. https://doi.org/10.1038/nsb0901-795.
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    • Benson, D. E., D. W. Conrad, R. M. de Lorimier, S. A. Trammell, and H. W. Hellinga. “Design of bioelectronic interfaces by exploiting hinge-bending motions in proteins.” Science 293, no. 5535 (August 31, 2001): 1641–44. https://doi.org/10.1126/science.1062461.
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    • Marvin, J. S., and H. W. Hellinga. “Conversion of a maltose receptor into a zinc biosensor by computational design.” Proc Natl Acad Sci U S A 98, no. 9 (April 24, 2001): 4955–60. https://doi.org/10.1073/pnas.091083898.
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    • Looger, L. L., and H. W. Hellinga. “Generalized dead-end elimination algorithms make large-scale protein side-chain structure prediction tractable: implications for protein design and structural genomics.” J Mol Biol 307, no. 1 (March 16, 2001): 429–45. https://doi.org/10.1006/jmbi.2000.4424.
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    • Trammell, S. A., H. M. Goldston, P. T. Tran, L. M. Tender, D. W. Conrad, D. E. Benson, and H. W. Hellinga. “Synthesis and characterization of a ruthenium(II)-based redox conjugate for reagentless biosensing.” Bioconjug Chem 12, no. 4 (2001): 643–47. https://doi.org/10.1021/bc010022q.
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    • Benson, D. E., M. S. Wisz, and H. W. Hellinga. “Rational design of nascent metalloenzymes.” Proc Natl Acad Sci U S A 97, no. 12 (June 6, 2000): 6292–97. https://doi.org/10.1073/pnas.97.12.6292.
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    • Sloan, D. J., and H. W. Hellinga. “Dissection of the protein G B1 domain binding site for human IgG Fc fragment.” Protein Sci 8, no. 8 (August 1999): 1643–48. https://doi.org/10.1110/ps.8.8.1643.
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    • Hellinga, H. W. “Construction of a blue copper analogue through iterative rational protein design cycles demonstrates principles of molecular recognition in metal center formation.” Journal of the American Chemical Society 120, no. 39 (October 7, 1998): 10055–66. https://doi.org/10.1021/ja980054x.
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    • Sloan, D. J., and H. W. Hellinga. “Structure-based engineering of environmentally sensitive fluorophores for monitoring protein-protein interactions.” Protein Eng 11, no. 9 (September 1998): 819–23. https://doi.org/10.1093/protein/11.9.819.
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    • Benson, D. E., M. S. Wisz, and H. W. Hellinga. “The development of new biotechnologies using metalloprotein design.” Curr Opin Biotechnol 9, no. 4 (August 1998): 370–76. https://doi.org/10.1016/s0958-1669(98)80010-4.
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    • Hellinga, H. W. “Computational protein engineering.” Nat Struct Biol 5, no. 7 (July 1998): 525–27. https://doi.org/10.1038/776.
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    • Wisz, M. S., C. Z. Garrett, and H. W. Hellinga. “Construction of a family of Cys2His2 zinc binding sites in the hydrophobic core of thioredoxin by structure-based design.” Biochemistry 37, no. 23 (June 9, 1998): 8269–77. https://doi.org/10.1021/bi980718f.
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    • Benson, D. E., M. S. Wisz, W. Liu, and H. W. Hellinga. “Construction of a novel redox protein by rational design: conversion of a disulfide bridge into a mononuclear iron-sulfur center.” Biochemistry 37, no. 20 (May 19, 1998): 7070–76. https://doi.org/10.1021/bi980583d.
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    • Hellinga, H. W., and J. S. Marvin. “Protein engineering and the development of generic biosensors.” Trends Biotechnol 16, no. 4 (April 1998): 183–89. https://doi.org/10.1016/s0167-7799(98)01174-3.
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    • Piervincenzi, R. T., W. M. Reichert, and H. W. Hellinga. “Genetic engineering of a single-chain antibody fragment for surface immobilization in an optical biosensor.” Biosens Bioelectron 13, no. 3–4 (March 1, 1998): 305–12. https://doi.org/10.1016/s0956-5663(97)00130-9.
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    • Marvin, J. S., and H. W. Hellinga. “Engineering biosensors by introducing fluorescent allosteric signal transducers: Construction of a novel glucose sensor.” Journal of the American Chemical Society 120, no. 1 (January 14, 1998): 7–11. https://doi.org/10.1021/ja972993f.
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    • Hellinga, H. W. “The construction of metal centers in proteins by rational design.” Fold Des 3, no. 1 (1998): R1–8. https://doi.org/10.1016/S1359-0278(98)00001-7.
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    • Hellinga, H. W. “Rational protein design: combining theory and experiment.” Proc Natl Acad Sci U S A 94, no. 19 (September 16, 1997): 10015–17. https://doi.org/10.1073/pnas.94.19.10015.
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    • Coldren, C. D., H. W. Hellinga, and J. P. Caradonna. “The rational design and construction of a cuboidal iron-sulfur protein.” Proc Natl Acad Sci U S A 94, no. 13 (June 24, 1997): 6635–40. https://doi.org/10.1073/pnas.94.13.6635.
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    • Pinto, A. L., H. W. Hellinga, and J. P. Caradonna. “Construction of a catalytically active iron superoxide dismutase by rational protein design.” Proc Natl Acad Sci U S A 94, no. 11 (May 27, 1997): 5562–67. https://doi.org/10.1073/pnas.94.11.5562.
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    • Marvin, J. S., E. E. Corcoran, N. A. Hattangadi, J. V. Zhang, S. A. Gere, and H. W. Hellinga. “The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors.” Proc Natl Acad Sci U S A 94, no. 9 (April 29, 1997): 4366–71. https://doi.org/10.1073/pnas.94.9.4366.
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    • De Lorimier, R., H. W. Hellinga, and L. D. Spicer. “NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin.” Protein Sci 5, no. 12 (December 1996): 2552–65. https://doi.org/10.1002/pro.5560051218.
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    • Hellinga, H. W. “Metalloprotein design.” Curr Opin Biotechnol 7, no. 4 (August 1996): 437–41. https://doi.org/10.1016/s0958-1669(96)80121-2.
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    • Ermácora, M. R., D. W. Ledman, H. W. Hellinga, G. W. Hsu, and R. O. Fox. “Mapping staphylococcal nuclease conformation using an EDTA-Fe derivative attached to genetically engineered cysteine residues.” Biochemistry 33, no. 46 (November 22, 1994): 13625–41. https://doi.org/10.1021/bi00250a013.
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    • Hellinga, H. W., and F. M. Richards. “Optimal sequence selection in proteins of known structure by simulated evolution.” Proc Natl Acad Sci U S A 91, no. 13 (June 21, 1994): 5803–7. https://doi.org/10.1073/pnas.91.13.5803.
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    • Ladbury, J. E., N. Kishore, H. W. Hellinga, R. Wynn, and J. M. Sturtevant. “Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry.” Biochemistry 33, no. 12 (March 29, 1994): 3688–92. https://doi.org/10.1021/bi00178a027.
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    • Ladbury, J. E., R. Wynn, H. W. Hellinga, and J. M. Sturtevant. “Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position.” Biochemistry 32, no. 29 (July 27, 1993): 7526–30. https://doi.org/10.1021/bi00080a026.
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    • Walker, D. S., H. W. Hellinga, S. S. Saavedra, and W. M. Reichert. “Integrated optical waveguide attenuated total reflection spectrometry and resonance Raman spectroscopy of adsorbed cytochrome c.” Journal of Physical Chemistry 97, no. 39 (January 1, 1993): 10217–22. https://doi.org/10.1021/j100141a051.
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    • Hellinga, H. W., R. Wynn, and F. M. Richards. “The hydrophobic core of Escherichia coli thioredoxin shows a high tolerance to nonconservative single amino acid substitutions.” Biochemistry 31, no. 45 (November 17, 1992): 11203–9. https://doi.org/10.1021/bi00160a034.
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    • Hellinga, H. W., J. P. Caradonna, and F. M. Richards. “Construction of new ligand binding sites in proteins of known structure. II. Grafting of a buried transition metal binding site into Escherichia coli thioredoxin.” J Mol Biol 222, no. 3 (December 5, 1991): 787–803. https://doi.org/10.1016/0022-2836(91)90511-4.
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    • Hellinga, H. W., and F. M. Richards. “Construction of new ligand binding sites in proteins of known structure. I. Computer-aided modeling of sites with pre-defined geometry.” J Mol Biol 222, no. 3 (December 5, 1991): 763–85. https://doi.org/10.1016/0022-2836(91)90510-d.
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    • Lau, F. T., A. R. Fersht, H. W. Hellinga, and P. R. Evans. “Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase.” Biochemistry 26, no. 13 (June 30, 1987): 4143–48. https://doi.org/10.1021/bi00387a060.
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    • Hellinga, H. W., and P. R. Evans. “Mutations in the active site of Escherichia coli phosphofructokinase.” Nature 327, no. 6121 (June 4, 1987): 437–39. https://doi.org/10.1038/327437a0.
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    • Hellinga, H. W., and P. R. Evans. “Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase.” Eur J Biochem 149, no. 2 (June 3, 1985): 363–73. https://doi.org/10.1111/j.1432-1033.1985.tb08934.x.
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