Faculty Profiles

Wilson, C., Lewis, K. A., Fitzkee, N. C., Hough, L. E., & Whitten, S. T. (2023). ParSe 2.0: A web tool to identify drivers of protein phase separation at the proteome level. Protein Science, 32(9). https://doi.org/doi: 10.1002/pro.4756

Yarawsky, A. E., Ori, A. L., English, L. R., Whitten, S. T., & Herr, A. B. (2023). Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns. Protein Science, 32(8). https://doi.org/10.1002/pro.4707

Ibrahim, A. Y., Khaodeuanepheng, N. P., Amarasekara, D. L., Correia, J. J., Lewis, K. A., Fitzkee, N. C., … Whitten, S. T. (2023). Intrinsically disordered regions that drive phase separation form a robustly distinct protein class. Journal of Biological Chemistry, 299(1), 102801. https://doi.org/10.1016/j.jbc.2022.102801

Paiz, E. A., Correia, J. J., Fitzkee, N. C., Hough, L. E., & Whitten, S. T. (2021). Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins. Journal of Biological Chemistry, 297(5). https://doi.org/10.1016/j.jbc.2021.101343

Paiz, E. A., Lewis, K. A., & Whitten, S. T. (2021). Structural and energetic characterization of the denatured state from the perspectives of peptides, the coil library, and intrinsically disordered proteins. Molecules, 26(3). https://doi.org/10.3390/molecules26030634

Tischer, A., Brehm, M. A., Machha, V. R., Moon-Tasson, L., Benson, L. M., Nelton, K. J., … Auton, M. (2020). Evidence for the Misfolding of the A1 Domain Within Multimeric Von Willebrand Factor in Type 2 Von Willebrand Disease. Journal of Molecular Biology, 432, 305–323. https://doi.org/doi.org/10.1016/j.jmb.2019.09.022

English, L. R., Voss, S. M., Tilton, E. C., Paiz, E. A., So, S., Parra, G. L., & Whitten, S. T. (2019). Impact of Heat on Coil Hydrodynamic Size Yields the Energetics of Denatured State Conformational Bias. Journal of Physical Chemistry B, 123(47), 10014–10024. https://doi.org/doi.org/10.1021/acs.jpcb.9b09088

English, L. R., Tischer, A., Demeler, A. K., Demeler, B., Auton, M., & Whitten, S. T. (2018). Sequence reversal prevents chain collapse and yields heat-sensitive intrinsic disorder. Biophysical Journal, 115(2), 328–340. https://doi.org/10.1016/j.bpj.2018.06.006

Yarawsky, A. E., English, L. R., Whitten, S. T., & Herr, A. B. (2017). The Proline/Glycine-Rich Region of the Biofilm Adhesion Protein Aap Forms an Extended Stalk that Resists Compaction. Journal of Molecular Biology, 429, 261–279. https://doi.org/10.1016/j.jmb.2016.11.017

English, L. R., Tilton, E. C., Ricard, B. J., & Whitten, S. T. (2017). Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins. Proteins: Structure, Function, and Bioinformatics, 85, 296–311. https://doi.org/10.1002/prot.25222

Tomasso, M. E., Tarver, M. J., Devarajan, D., & Whitten, S. T. (2016). Hydrodynamic radii of intrinsically disordered proteins determined from experimental polyproline II propensities. PLoS Computational Biology, 12(1), 1e1004686. https://doi.org/doi:10.1371/journal.pcbi.1004686

Dasari, R., Masi, M., Lisy, R., Ferdérin, M., English, L. R., Cimino, A., … Kornienko, A. (2015). Fungal metabolite ophiobolin A as a promising anti-glioma agent: in vivo evaluation, structure-activity relationship and unique pyrrolylation of primary amines. Bioorganic & Medicinal Chemistry Letters, 25, 4544–4548. https://doi.org/10.1016/j.bmcl.2015.08.066

Zimmermann, M. T., Tischer, A., Whitten, S. T., & Auton, M. (2015). Structural origins of misfolding propensity in the platelet adhesive VWF A1 domain. Biophysical Journal, 109, 398–406. https://doi.org/doi: 10.1016/j.bpj.2015.06.008

Hilser, V. J., & Whitten, S. T. (2014). Using the COREX/BEST Server to model the native state ensemble. Methods in Molecular Biology, 1084, 255–269. https://doi.org/10.1007/978-1-62703-658-0_14

Perez, R. B., Tischer, A., Auton, M., & Whitten, S. T. (2014). Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins. Proteins: Structure, Function, and Bioinformatics, 82, 3373–3384. https://doi.org/10.1002/prot.24692

Langridge, T. D., Tarver, M. J., & Whitten, S. T. (2014). Temperature effects on the hydrodynamic radius of the intrinsically disordered N-terminal region of the p53 protein. Proteins: Structure, Function, and Bioinformatics, 82, 668–678. https://doi.org/10.1002/prot.24449

Schaub, L. J., Campbell, J. C., & Whitten, S. T. (2012). Thermal unfolding of the N-terminal region of p53 monitored by circular dichroism spectroscopy. Protein Science, 21, 1682–1688. https://doi.org/10.1002/pro.2146

Campbell, J. C., & Whitten, S. T. (2012). Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble. Proteins: Structure, Function, and Bioinformatics, 80, 184–193. https://doi.org/10.1002/prot.23178

Wrabl, J. O., Gu, J., Liu, T. 1016/j. bpc. 2011. 05. 020, Schrank, T. P., Whitten, S. T., & Hilser, V. J. (2011). The role of protein conformational fluctuations in allostery, function, and evolution. Biophysical Chemistry, 159, 129–141. https://doi.org/10.1016/j.bpc.2011.05.020

Bell-Upp, P., Robinson, A. C., Whitten, S. T., Wheeler, E. L., Lin, J., Stites, W. E., & García-Moreno, B. (2011). Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins. Biophysical Chemistry, 159, 217–226. https://doi.org/10.1016/j.bpc.2011.06.016

Hilser, V. J., & Whitten, S. T. (2009). Energy flow and allostery in an ensemble. In Proteins: Energy, Heat, and Signal Flow (pp. 341–360). CRC Press.

Manson, A., Whitten, S. T., Ferreon, J. C., Fox, R. O., & Hilser, V. J. (2009). Characterizing the role of ensemble modulation in mutation-induced changes in binding affinity. Journal of the American Chemical Society, 131, 6785–6793. https://doi.org/10.1021/ja809133u

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. In Unfolded proteins: from denatured states to intrinsically disordered (pp. 169–193). Nova Science Publishers, Inc.

Whitten, S. T., García-Moreno, 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 Biology, 84, 871–891. https://doi.org/10.1016/S0091-679X(07)84027-1

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. Journal of Molecular Biology, 381, 1184–1201. https://doi.org/10.1016/j.jmb.2008.06.046

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 Science, 17, 1200–1211. https://doi.org/10.1110/ps.033647.107

Liu, T., Whitten, S. T., & 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. https://doi.org/10.1073/pnas.0607132104

Whitten, S. T., Kurtz, A. J., Pometun, M. S., Wand, A. J., & Hilser, V. J. (2006). Revealing the nature of the native state ensemble through cold denaturation. Biochemistry, 45, 10163–10174. https://doi.org/10.1021/bi060855+

Hilser, V. J., García-Moreno, B., Oas, T. G., Kapp, G., & Whitten, S. T. (2006). A statistical thermodynamic model of the protein ensemble. Chemical Reviews, 106, 1545–1558. https://doi.org/10.1021/cr040423+

Fitch, C. A., Whitten, S. T., Hilser, V. J., & García-Moreno, B. (2006). Molecular mechanisms of pH-driven conformational transitions of proteins: Insights from continuum electrostatics calculations of acid unfolding. Proteins: Structure, Function, and Bioinformatics, 63, 113–126. https://doi.org/10.1002/prot.20797

Liu, T., Whitten, S. T., & Hilser, V. J. (2006). Ensemble-based signatures of energy propagation in proteins: a new view of an old phenomenon. Proteins: Structure, Function, and Bioinformatics, 62, 728–738. https://doi.org/10.1002/prot.20749

Olmsted, S. S., Khanna, K. V., Ng, E. M., Whitten, S. T., Johnson, O. N., Markham, R. B., … Moench, T. R. (2005). Low pH immobilizes and kills human leukocytes and prevents transmission of cell-associated HIV in a mouse model. BMC Infectious Diseases, 5, 79–87. https://doi.org/10.1186/1471-2334-5-79

Vertrees, J., Barritt, P., Whitten, S. T., & Hilser, V. J. (2005). COREX/BEST server: a web browser-based program that calculates regional stability variations within protein structures. Bioinformatics, 21, 3318–3319. https://doi.org/10.1093/bioinformatics/bti520

Whitten, S. T., García-Moreno, B., & 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. https://doi.org/10.1073/pnas.0407499102

Hamburger, J. B., Ferreon, J. C., Whitten, S. T., & 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. https://doi.org/10.1021/bi049352z

Whitten, S. T., Wooll, J. O., Razeghifard, R., Garcı́a-Moreno, E. B., & Hilser, V. J. (2001). The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins. Journal of Molecular Biology, 309(5), 1165–1175. https://doi.org/10.1006/jmbi.2001.4726

Whitten, S. T., & García-Moreno, B. (2000). pH dependence of stability of staphylococcal nuclease: evidence of substantial electrostatic interactions in the denatured state. Biochemistry, 39, 14292–14304. https://doi.org/10.1021/bi001015c