Biochemistry and Molecular Biology
Penn State Science
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Scott Showalter

Scott Showalter

Main Content

  • Associate Professor of Chemistry and Associate Professor of Biochemistry and Molecular Biology
106 Chemistry Building
University Park, PA 16802
Email: sas76@psu.edu
Phone: (814) 865-2318

Research Interests

Analytical, Biological, Computational/Theoretical, Physical, Biomedical

Graduate Programs

BMMB, CHEMMCIBS

Information

Biophysical Chemistry applied to solution NMR spectroscopy of partially disordered proteins. NMR studies of protein dynamics coupled with computational and theoretical studies of the coupling between nuclear spin relaxation and molecular motion. Emphasis is placed on biophysical studies of macromolecular interactions involving partially disordered proteins, for the purpose of understanding the functional implications of protein dynamics and disorder in protein mediated signaling and oncogenesis/ tumor suppression.

Dynamics and Disorder in Protein Ligand Interactions

Proteins are dynamic molecules and developing an intuitive understanding of the relationship between structure, dynamics, and function is a universally valuable goal. The primary research tools used by members of our laboratory are Nuclear Magnetic Resonance spectroscopy (NMR), molecular dynamics simulations (MD), and Isothermal Titration Calorimetry (ITC). Since our emphasis is on studying interactions involving disordered proteins and flexible agonists, the focus of the work is on the conformational dynamics of proteins and the contributions of these dynamics to protein-protein interactions. For flexible systems with disorder-order transitions coupled to the binding event, NMR spectroscopy remains the most powerful source of atomic level biophysical information available, with access to dynamics on the fast ps-ns timescale, as well as the biologically critical μs-ms timescale.  Shifting focus from backbone to side chain NMR dynamics further broadens the possibilities for understanding protein-protein interactions and non-folded systems.  Combined analysis of experimental NMR data and computational results provides a uniquely detailed picture of correlated dynamics. Rigorous protocols for cross validation of MD trajectories and theoretical calculations against diverse experimental NMR data are applied throughout the projects in our laboratory.


Selected Publications

  • Gibbs, E.B., & Showalter, S.A. (2015) “Quantitative Biophysical Characterization of Intrinsically Disordered Proteins.” Biochemistry, 54, 1314-1326.
  • Acevedo, R., Orench-Rivera, N., Quarles, K.A., & Showalter, S.A. (2015) “Helical Defects in MicroRNA Influence Protein Binding by TAR RNA Binding Protein.” PLoS One, 10, e0116749. PMCID: In Process
  • Cordek, D.G., Croom-Perez, T.J., Hwang, J., Hargittai, M.R.S., Subba-Reddy, C.V., Han, Q., Lodeiro, M.F., Ning, G., McCrory, T.S., Arnold, J.J., Koc, H., Lindenbach, B.D., Showalter, S.A., & Cameron, C.E. (2014) “Expanding the proteome of an RNA virus by phosphorylation of an intrinsically disordered viral protein.” J. Biol. Chem., 289, 24397-24416. PMCID: In Process
  • Showalter, S.A. (2014) “Intrinsically Disordered Proteins: Methods for Structure and Dynamics Studies.” eMagRes, 3, 181-190.
  • Lawrence, C.W., Kumar, S., Noid, W.G., & Showalter, S.A. (2014) “The Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins.” J. Phys. Chem. Lett., 5, 833-838.
  • Sahu, D., Bastidas, M., & Showalter, S.A. (2014) “Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.” Anal. Biochem., 449, 17-25. PMCID: PMC3944900

Honors and Awards

  • Eastern Analytical Symposium New Faculty Award in NMR Spectroscopy, 2012
  • NSF Career Award, 2010.
  • NIH Ruth L. Kirschstein NRSA Postdoctoral Fellow 2005-2008.
  • NSF Predoctoral Fellow 2000-2003.