Steven T. Whitten, Ph.D.

2000 Johns Hopkins University, Baltimore, MD 
General Biophysics, Biochemistry
"Steven Whitten"
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Bertrand Garcia-Moreno grad student 2000 Johns Hopkins
 (Acid denaturation and pH dependence of stability of staphylococcal nuclease.)
Michael Blaber post-doc 1999-2000 Florida State
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Tomasso ME, Tarver MJ, Devarajan D, et al. (2016) Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities. Plos Computational Biology. 12: e1004686
Zimmermann MT, Tischer A, Whitten ST, et al. (2015) Structural Origins of Misfolding Propensity in the Platelet Adhesive von Willebrand Factor A1 Domain Biophysical Journal. 109: 398-406
Dasari R, Masi M, Lisy R, et al. (2015) Fungal metabolite ophiobolin A as a promising anti-glioma agent: In vivo evaluation, structure-activity relationship and unique pyrrolylation of primary amines Bioorganic and Medicinal Chemistry Letters
Perez RB, Tischer A, Auton M, et al. (2014) Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins. Proteins. 82: 3373-84
Langridge TD, Tarver MJ, Whitten ST. (2014) Temperature effects on the hydrodynamic radius of the intrinsically disordered N-terminal region of the p53 protein. Proteins. 82: 668-78
Hilser VJ, Whitten ST. (2014) Using the COREX/BEST server to model the native-state ensemble. Methods in Molecular Biology (Clifton, N.J.). 1084: 255-69
Schaub LJ, Campbell JC, Whitten ST. (2012) Thermal unfolding of the N-terminal region of p53 monitored by circular dichroism spectroscopy. Protein Science : a Publication of the Protein Society. 21: 1682-8
Campbell JC, Whitten ST. (2012) Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble. Proteins. 80: 184-93
Bell-Upp P, Robinson AC, Whitten ST, et al. (2011) Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins. Biophysical Chemistry. 159: 217-26
Wrabl JO, Gu J, Liu T, et al. (2011) The role of protein conformational fluctuations in allostery, function, and evolution. Biophysical Chemistry. 159: 129-41
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