Publications

Preprints in bioRxiv: (* indicates corresponding author)

  1. Maguire, L.; Reskin, S.; Wall, K.; Arroyo, E.; Marchando, P.; Whited, A. M.; Erbse, A.; Whitten, S. T.; Hough, L. E.* Aggregation of an FG nucleoporin under crowded conditions. bioRxiv. 2024, doi: 10.1101/2024.04.15.589310.

Chapters in books:

  1. Hilser, V. J.; Whitten, S. T. Energy flow and allostery in an ensemble. In Proteins: Energy, Heat, and Signal Flow; CRC Press, 2009; pp 341-360.
  2. Whitten, S. T.; Ferreon, J. C.; Hamburger, J. B.; Hilser, V. J. 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; Nova Science Publishers, Inc, 2008; pp 169-193.

Refereed journal articles:  (* indicates corresponding author)

  1. Wilson, C.; Lewis, K. A.; Fitzkee, N. C.; Hough, L. E.; Whitten, S. T.* ParSe 2.0: A web tool to identify drivers of protein phase separation at the proteome level. Protein Sci. 2023, 32, e4756.
  2. Yarawsky, A. E.; Ori, A. L.; English, L. R.; Whitten, S. T.; Herr, A. B.* Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns. Protein Sci. 2023, 32, e4707.
  3. Ibrahim, A. Y.; Khaodeuanepheng, N. P.; Amarasekara, D. L.; Correia, J. J.; Lewis, K. A.; Fitzkee, N. C.; Hough, L. E.*; Whitten, S. T.* Intrinsically disordered regions that drive phase separation form a distinctly robust protein class. J. Biol. Chem. 2023, 299, 102801.
  4. Paiz, E. A.; Allen, J. H.; Correia, J. J.; Fitzkee, N. C.; Hough, L. E.; Whitten, S. T.* Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins. J. Biol. Chem. 2021, 297, 101343.
  5. Paiz, E. A.; Lewis, K. A.; Whitten, S. T.* Structural and energetic characterization of the denatured state from the perspectives of peptides, the coil library, and intrinsically disordered proteins. Molecules 2021, 26, 634.
  6. Tischer A.; Brehm, M. A.; Machha, V. R.; Moon-Tasson, L.; Benson, L. M.; Nelton, K. J.; Leger, R. R.; Obserm, T.; Martinez-Vargas, M.; Whitten, S. T.; Chen, D.; Pruthi, R. K.; Bergen, H. R.; Cruz, M. A.; Schneppenheim, R.; Auton, M.* Evidence for the Misfolding of the A1 Domain within Multimeric Von Willebrand Factor in Type 2 Von Willebrand Disease. J. Mol. Biol. 2020, 432, 305-323.
  7. English, L. R.; Voss, S. M.; Tilton, E. C.; Paiz, E. A.; So, S.; Parra, G. R.; Whitten, S. T.* Impact of heat on coil hydrodynamic size yields the energetics of denatured state conformational bias. J. Phys. Chem. B 2019, 123, 10014-10024.
  8. English, L. R.; Tischer, A.; Demeler, A. K.; Demeler, B.; Whitten, S. T.* Sequence reversal prevents chain collapse and yields heat-sensitive intrinsic disorder. Biophys. J. 2018, 115, 328-340.
  9. English, L. R.; Tilton, E. C.; Ricard, B. J.; Whitten, S. T.* Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins. Proteins 2017, 85, 296-311.
  10. Yarawsky, A. E.; English, L. R.; Whitten, S. T.; Herr, A. B.* The proline/glycine-rich region of the biofilm adhesion protein aap forms an extended stalk that resists compaction. J. Mol. Biol. 2017 429, 261-279.
  11. Tomasso, M. E.; Tarver, M. J.; Devarajan, D.; Whitten, S. T.* Hydrodynamic radii of intrinsically disordered proteins determined from experimental polyproline II propensities. PLoS Comput. Biol. 2016 12(1):e1004686.
  12. Dasari, R.; Masi, M.; Lisy, R.; Ferdérin, M.; English, L. R.; Cimino, A.; Mathieu, V.; Brenner, A. J.; Kuhn, J. G.; Whitten, S. T.; Evidente, A.; Kiss, R.; Kornienko, A.* Fungal metabolite ophiobolin A as a promising anti-glioma agent: in vivo evaluation, structure-activity relationship and unique pyrrolylation of primary amines. Bioorg. Med. Chem. Lett. 2015 25, 4544-4548.
  13. Zimmermann, M.; Tischer, A.; Whitten, S. T.; Auton, M.* Structural origins of misfolding propensity in the platelet adhesive VWF A1 domain. Biophys. J. 2015, 109, 398-406.
  14. Perez, R; Tischer, A.; Auton, M.; Whitten, S. T.* Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins. Proteins 2014, 82, 3373-3384.
  15. Langridge, T. D.; Tarver, M. J.; Whitten, S. T.* Temperature effects on the hydrodynamic radius of the intrinsically disordered N-terminal region of the p53 protein. Proteins 2014, 82, 668-678.
  16. Hilser, V. J.; Whitten, S. T.* Using the COREX/BEST Server to model the native state ensemble. Methods Mol. Biol. 2014, 1084, 255-269.
  17. Schaub, L. J.; Campbell, J. C.; Whitten, S. T.* Thermal unfolding of the N-terminal region of p53 monitored by circular dichroism spectroscopy. Protein Sci. 2012, 21, 1682-1688.
  18. Campbell, J. C.; Whitten, S. T.* Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble. Proteins 2012, 80, 184-193.
  19. Wrabl, J. O.; Gu, J.; Liu, T.; Schrank, T. P.; Whitten, S. T.; Hilser, V. J.* The role of protein conformational fluctuations in allostery, function, and evolution. Biophys. Chem. 2011, 159, 129-141.
  20. Bell-Upp, P.; Robinson, A. C.; Whitten, S. T.; Wheeler, E. L.; Lin, J.; Stites, W. E.; García-Moreno E., B.* Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins. Biophys. Chem. 2011, 159, 217-226.
  21. Manson, A. C.; Whitten, S. T.; Ferreon, J. C.; Fox, R. O.; Hilser, V. J.* Characterizing the role of ensemble modulation in mutation-induced changes in binding affinity. J. Am. Chem. Soc. 2009, 131, 6785-6793.
  22. Wang, S.; Gu, J.; Larson, S. A.; Whitten, S. T.; Hilser, V. J.* Denatured-state energy landscapes of a protein structural database reveal the energetic determinants of a framework model for folding. J. Mol. Biol. 2008, 381, 1184-1201.
  23. Whitten, S. T.; Yang, H. W.; Fox, R. O.; Hilser, V. J.* Exploring the impact of conformational bias on the binding of peptides to the SEM-5 SH3 domain. Protein Sci. 2008, 17, 1200-1211.
  24. Whitten, S. T.; García-Moreno E., B.; Hilser, V. J.* Ligand effects on the protein ensemble: unifying the descriptions of ligand binding, local conformational fluctuations, and protein stability. Methods Cell Biol. 2008, 84, 871-891.
  25. Liu, T.; Whitten, S. T.; Hilser, V. J.* Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble. Proc. Natl. Acad. Sci. USA 2007, 104, 4347-4352.
  26. Whitten, S. T.; Kurtz, A. J.; Pometun, M. S.; Wand, J. A.; Hilser, V. J.* Revealing the nature of the native state ensemble through cold denaturation. Biochemistry 2006, 45, 10163-10174.
  27. Fitch, C. A.; Whitten, S. T.; Hilser, V. J.; García-Moreno E., B.* Molecular mechanisms of pH-driven conformational transitions of proteins: Insights from continuum electrostatics calculations of acid unfolding. Proteins 2006, 63, 113-126.
  28. Liu, T.; Whitten, S. T.; Hilser, V. J.* Ensemble-based signatures of energy propagation in proteins: a new view of an old phenomenon. Proteins 2006, 62, 728-738.
  29. Hilser, V. J.*; García-Moreno E., B.; Oas, T. G.; Kapp, G.; Whitten, S. T. A statistical thermodynamic model of the protein ensemble. Chem. Rev. 2006, 106, 1545-1558.
  30. Whitten, S. T.; García-Moreno E., B.; Hilser, V. J.* Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins. Proc. Natl. Acad. Sci. USA 2005, 102, 4282-4287.
  31. Vertrees, J.; Barritt, P.; Whitten, S. T.; Hilser, V. J.* COREX/BEST server: a web browser-based program that calculates regional stability variations within protein structures. Bioinform. 2005, 21, 3318-3319.
  32. Olmsted, S. S.; Khanna, K. V.; Ng, E. M.; Whitten, S. T.; Johnson, O. N. III; Markham, R. B.; Cone, R. A.; Moench, T. R.* Low pH immobilizes and kills human leukocytes and prevents transmission of cell-associated HIV in a mouse model. BMC Infect. Dis. 2005, 5, 79-87.
  33. Hamburger, J. B.; Ferreon, J. C.; Whitten, S. T.; Hilser, V. J.* Thermodynamic mechanisms and consequences of the polyproline II (PII) structural bias in the denatured states of proteins. Biochemistry 2004, 43, 9790-9799.
  34. Whitten, S. T.; Wooll, J. O.; Razeghifard, R.; García-Moreno E., B.; Hilser, V. J.* The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins. J. Mol. Biol. 2001, 309, 1165-1175.
  35. Whitten, S. T.; García-Moreno E., B.* pH dependence of stability of staphylococcal nuclease: evidence of substantial electrostatic interactions in the denatured state. Biochemistry 2000, 39, 14292-14304.

Experimental and Computational Biophysics