||Wednesday, April 10, 2013
405 - Combined isothermal titration calorimetry and fluorescence stopped flow study of the DNA threading mechanism of nogalamycin
Samantha Glazier, email@example.com, Department of Chemistry, St. Lawrence University, Canton, ny 13617, United States
ITC has been routinely applied to investigate protein binding, an equilibrium where heat changes due to binding are large enough to be easily distinguished from heats of dilution. One of the challenges of analyzing DNA binding data correctly is accounting for background signals that can be quite large. The conjugated ring system of nogalamycin is a common feature of small molecules that bind between the base pairs of DNA. The conjugated rings also facilitate dimer formation, which contribute significantly to heats of dilution in ITC experiments. Niklaas J. Buurma and co-authors have written a publically available program to account for significant sources of heat such as that due to dimer formation. The thermodynamics of binding for the nogalamycin DNA reaction will be investigated using this detailed accounting of heats of dilution and then be compared to data from a Van t' Hoff analysis. Fluorescence titration data for the association and dissociation reactions will be presented as well. The combined thermodynamic and kinetics data will give a complete picture of the binding mechanism that ultimately finds nogalamycin threaded between the base pairs of DNA despite being too large to simply pass though.
Wednesday, April 10, 2013 06:00 PM
PHYS Poster Session (06:00 PM - 09:00 PM)
Location: Morial Convention Center
Room: Hall D
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