| Schaub, L.J., Campbell, J. C., and Whitten, S. T. (2012) “Thermal unfolding of the N-terminal region of p53 monitored by circular dichroism spectroscopy.” Protein Science, 21, 1682-1688. |
| Campbell, J. C., and Whitten, S. T. (2012) “Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble.” Proteins, 80, 184-193. (Epub: Sept 14 2011). |
| Wrabl, J. O., Gu, J., Liu, T., Schrank, T. P., Whitten, S. T., and Hilser, V. J. (2011) “The role of protein conformational fluctuations in allostery, function, and evolution.” Biophys. Chem., 159, 129-141. |
| Bell-Upp, P., Robinson, A. C., Whitten, S. T., Wheeler, E. L., Lin, J., Stites, W. E., and García-Moreno E., B. (2011) “Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins.” Biophys. Chem., 159, 217-226 |
| Hilser, V. J., and Whitten, S. T. (2009). “Energy flow and allostery in an ensemble.” Proteins: Energy, Heat, and Signal Flow, CRC Press (ch 15, p341-360). |
| Manson, A. C., Whitten, S. T., Ferreon, J. C., Fox, R. O., and Hilser, V. J. (2009) “Characterizing the role of ensemble modulation in mutation-induced changes in binding affinity.” J. Am. Chem. Soc., 131, 6785-6793. |
| Wang, S., Gu, J., Larson, S. A., Whitten, S. T., Hilser, V. J. (2008) “Denatured-state energy landscapes of a protein structural database reveal the energetic determinants of a framework model for folding.” J. Mol. Biol. 381, 1184-1201. |
| Whitten, S. T., Yang, H. W., Fox, R. O., Hilser, V. J. (2008). “Exploring the impact of conformational bias on the binding of peptides to the SEM-5 SH3 domain.” Protein Sci. 17, 1200-1211. |
| Whitten, S. T., García-Moreno E., B., Hilser, V. J. (2008). “Ligand effects on the protein ensemble: unifying the descriptions of ligand binding, local conformational fluctuations, and protein stability.” Methods in Cell Biol. 84, 871-891. |
| Whitten, S. T., Ferreon, J. C., Hamburger, J. B., Hilser, V. J. (2008). “Calorimetric determination of the thermodynamics of polyproline II (PII) helix formation in the unfolded states of protein.” Unfolded proteins: from denatured states to intrinsically disordered, Nova Science Publishers, Inc (ch 7, p169-193). |
| Liu, T., Whitten, S. T., and Hilser, V. J. (2007). “Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble.” Proc. Natl. Acad. Sci. USA 104, 4347-4352. |
| Whitten, S. T., Kurtz, A. J., Pometun, M. S., Wand, J. A., and Hilser, V. J. (2006). “Revealing the nature of the native state ensemble through cold denaturation.” Biochemistry 45, 10163-10174. |
| Fitch, C. A., Whitten, S. T., Hilser, V. J., and García-Moreno E., B. (2006). “Molecular mechanisms of pH-driven conformational transitions of proteins: Insights from continuum electrostatics calculations of acid unfolding.” Proteins 63, 113-126. |
| Liu, T., Whitten, S. T., and Hilser, V. J. (2006). "Ensemble-based signatures of energy propagation in proteins: a new view of an old phenomenon.” Proteins 62, 728-738. |
| Hilser, V. J., García-Moreno E., B., Oas, T. G., Kapp, G., and Whitten, S. T. (2006). “A statistical thermodynamic model of the protein ensemble.” Chem. Rev. 106, 1545-1558. |
| Whitten, S. T., García-Moreno E., B., and Hilser, V. J. (2005). “Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.” Proc. Natl. Acad. Sci. USA 102, 4282-4287. |
| Vertrees, J., Barritt, P., Whitten, S. T., and Hilser, V. J. (2005). “COREX/BEST server: a web browser-based program that calculates regional stability variations within protein structures.” Bioinform. 21, 3318-3319. |
| Olmsted, S. S., Khanna, K. V., Ng, E. M., Whitten, S. T., Johnson, O. N. III, Markham, R. B., Cone, R. A., and Moench, T. R. (2005). “Low pH immobilizes and kills human leukocytes and prevents transmission of cell-associated HIV in a mouse model.” BMC Infect. Dis. 5, 79-87. |
| Hamburger, J. B., Ferreon, J. C., Whitten, S. T., and Hilser, V. J. (2004). “Thermodynamic mechanisms and consequences of the polyproline II (PII) structural bias in the denatured states of proteins.” Biochemistry 43, 9790-9799. |
| Whitten, S. T., Wooll, J. O., Razeghifard, R., García-Moreno E., B., and Hilser, V. J. (2001). “The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins.” J. Mol. Biol. 309, 1165-1175. |
| Whitten, S. T., and García-Moreno E., B. (2000). “pH dependence of stability of staphylococcal nuclease: evidence of substantial electrostatic interactions in the denatured state.” Biochemistry 39, 14292-14304. |
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