In general, what I am most fascinated by is protein structure. More specifically, how that structure dictates function and biomolecular recognition, and what happens when that structure is altered in diseased states. The techniques that my group uses to monitor and determine protein structure are circular dichroism (CD), fluorescence, and nuclear magnetic resonance (NMR) spectroscopy. Students working in my lab are involved in the production of protein (cloning, mutagenesis, over-expression), its purification, and its biophysical characterization. I encourage interested students to come and talk with me.
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*Fisher, S.; *Weck, M.; *Landers, J.; *Emrich, J.; *Middleton, S.; *Cox, J.; Gentile, L.N.; and Parish, C.A. “Theoretical and experimental evidence that the kinesin light chain is a tetratricopeptide repeat.” The Journal of Structural Biology, 2012,177, 602.
Gentile, L.;Caudill, L.; Fetea, M.; Hill, A.; Hoke, K.; Lawson, B.; Lipan, O.; Kerckhove, M.; Parish, C.; Stenger, K.; and Szajda, D. “Integrated Quantitative Science (IQS): Teaching Concepts from Biology, Chemistry, Computer Science, Mathematics and Physics in a Year-Long Introductory Course for First Year STEM Majors.” Journal of College Science Teaching, 2012, 41, 24.
Gentile, L.N.; and Hoke, K. “Using Global Problems as a Basis for an Integrated STEM Course for First-Year Students.” AAC&U Diversity & Democracy, 2011, 14, 2, 15.