Publications

Fei Li, Patricia B. Lutz, Yuliya Pepelyayeva, Elias S.J. Arner, Craig A. Bayse and Sharon Rozovsky.  Redox active motifs in selenoproteins (Submitted).

Sharon Rozovsky. ⁷⁷Se NMR spectroscopy of selenoproteins (Submitted).

Jun Liu, Fei Li and Sharon Rozovsky. The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro. Biochemistry 52 (18), 3051–3061(2013) http://dx.doi.org/10.1021/bi4001358

Stephanie A. Schaefer, Ming Dong, Renee P. Rubenstein, Wayne A. Wilkie, Brian J. Bahnson, Colin Thorpe and Sharon Rozovsky. ⁷⁷Se Enrichment of Proteins Expands the Biological NMR Toolbox. Journal of Molecular Biology 425, 222-231 (2013) http://dx.doi.org/10.1016/j.jmb.2012.11.011

See a concise explanation at http://thorpelab.chem.udel.edu/index.php/blog/114-expanding-the-biological-nmr-toolbox

Jun Liu, Prabha Srinivasan, Diane N. Pham and Sharon Rozovsky. Expression and purification of the membrane enzyme selenoprotein K. Protein Expression and Purification 86 (1), 27–34 (2012) http://dx.doi.org/10.1016/j.pep.2012.08.014

Rozovsky, S., Forstner, M.B., Sondermann, H. and Groves, J. T. Binding kinetics of Epsin N-terminal Homology (ENTH) to lipid bilayers measured by single molecule total internal reflection microscopy. Journal of Physical Chemistry 116 (17), 5122-5131 (2012). http://dx.doi.org/10.1021/jp210045r

Jochem Struppe, Barry Dunietz and Sharon Rozovsky. ⁷⁷Se chemical shift tensor of L-selenocystine (In preparation).

Yuliya Pepelyayeva and Sharon Rozovsky. ⁷⁷Se as a probe of methionine’s role in ligand recognition, metal binding, and protein-protein interactions (In preparation).

Rozovsky, S. & McDermott, A. E. Substrate product equilibrium on a reversible enzyme: NMR detection for triosephosphate isomerase. Proceedings of the National Academy of Sciences 104 (7), 2080-2085 (2007). http://dx.doi.org/10.1073/pnas.0608876104

Rozovsky, S., Kaizuka, Y. & Groves, J. T. Formation and spatio-temporal evolution of periodic structures in lipid bilayers. Journal of the American Chemical Society 127 (1), 36-37 (2005). http://dx.doi.org/10.1021/ja046300o

Desamero, R, Rozovsky, S., Zhadin, N., McDermott, A. E. & Callender, R. Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation. Biochemistry 42 (10), 2941-2951 (2003). http://dx.doi.org/10.1021/bi026994i

Jogl, G., Rozovsky, S., McDermott, A. E. & Tong, L. Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution. Proceedings of the National Academy of Sciences 100, 50-55 (2003). http://dx.doi.org/10.1073/pnas.0233793100

Rozovsky, S., Jogl, G., Tong, L. & McDermott, A. E. Solution-state NMR investigations of triosephosphate isomerase active site motion: ligand release in relation to active site loop dynamics. Journal of Molecular Biology 310, 271-280 (2001). http://dx.doi.org/10.1006/jmbi.2001.4673

Rozovsky, S. & McDermott, A. E. The timescale of a catalytic loop motion in triosephosphate isomerase. Journal of Molecular Biology 310, 259-270 (2001). http://dx.doi.org/10.1006/jmbi.2001.4672