Calculation and Analysis of Enzyme Bimodal Stability Curves from

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Calculation and Analysis of Enzyme Bimodal Stability Curves from Novel Applications of Differential Scanning Calorimetry PI: Billy Mark Britt, Ph.D. Undergraduate Student Investigators: Melissa Bodnar, Heather Hollowell, Opral Ijeoma, Stacey McNevin, Duong Nguyen, Saronya Younvanich Department of Chemistry and Physics, Texas Woman’s University, Denton, TX 76204 An enzyme stability curve is a plot of the unfolding free energy ΔG(u) versus temperature. We have discovered that when care is taken to include unfolding data over a broad temperature range the existence of a nondenaturational conformational change is revealed in three of the four enzymes we have studied. These transition temperatures occur between the organism optimal thriving temperature and the temperature where crystals were grown for x-ray structure analysis. Two examples (yeast phosphoglycerate kinase (left) and bovine carbonic anhydrase (right)) are shown below. The stability curves were calculated from a combination of isothermal titrations with guanidine hydrochloride and from thermodynamic parameters obtained from differential scanning calorimetry measurements of unfolding obtained under reversible conditions (in the presence of guanidine hydrochloride). Acknowledgment is made to the Donors of the American Chemical Society Petroleum Research Fund for support of this research.