Scott Showalter
- Assistant Professor of Chemistry
University Park, PA 16802
Email: sas76@psu.edu
(814) 865-2318
Web Sites:
Education:
- B.S. Cornell University, Ithaca 1999.
- Ph.D. Washington University School of Medicine, St. Louis 2004.
- Postdoc National High Magnetic Field Laboratory, Tallahassee 2005-2008.
Honors and Awards:
- NSF Career Award, 2010.
- NIH Ruth L. Kirschstein NRSA Postdoctoral Fellow 2005-2008.
- NSF Predoctoral Fellow 2000-2003.
Selected Publications:
Representative Publications
Lawrence, C.W., Bonny, A., & Showalter, S.A. (2011) "The Disordered C-Terminus of the RNA Polymerase II Phosphatase FCP1 is Partially Helical in the Unbound State." Biochem. Biophys. Res. Comm., 410, 461-465.
O'Hare, B., Benesi, A.J., & Showalter, S.A. (2009) "Incorporating 1H Chemical Shift Determination into 13C-Detected Spectroscopy of Intrinsically Disordered Proteins in Solution." J. Mag. Reson., 200, 354-358.
Showalter, S.A. (2009) “NMR Assignment of the Intrinsically Disordered C-terminal Region of Homo sapiens FCP1 in the Unbound State.” Biomol. NMR Assign., 3, 179-181.
Levine, L.A., Kirin, S.I., Myers, C.P., Showalter, S.A., & Williams, M.E. (2009) “Heterometallic Ferrocene-Rhenium Complexes Linked by an Aminoethylglycine Scaffold.” Eur. J. Inorg. Chem., 2009, 613-621.
Wostenberg, C., Quarles, K.A., & Showalter, S.A. (2010) "Dynamic Origins of Differential RNA Binding Function in Two dsRBDs from the miRNA 'Microprocessor' Complex." Biochemistry, 49, 10728-10736.
Wostenberg, C. & Showalter, S.A. (2010) "MD Simulations of the dsRBP DGCR8 Reveal Correlated Motions that may Facilitate pri-miRNA Binding." Biophys. J., 99, 248-256.
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.
Research Interests:
- Analytical
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Biomolecular NMR spectroscopy, calorimetry studies of biomolecular systems.
- Biological
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Biophysical chemistry, macromolecular structure and dynamics by NMR
- Computational / Theoretical
- Physical
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NMR spectroscopy and methods development, simulation of biological systems.
- Bioanalytical
- Biophysical
- Spectroscopy
- Bio Structure/Function
- Biomedical
