Abstract
Thermal and stability properties of B17, the 17 % N-terminal domain of apo B, were carried out using differential scanning calorimetry spectroscopy, where the thermal characteristics of the polypeptide were studied and analyzed. The heat capacity data of B17 showed that the protein undergoes two transitions between 50 and 90 °C, with T m’s at 65.9 and 74.8 °C. While the first transition showed immediate reversibility, the second one—with the higher T m—necessitated a longer cooling (several days) period for its reversibility to be observed and both transitions could be seen in the heat capacity profile of B17. Moreover, the van’t Hoff enthalpies determined via calorimetric measurements agreed with the values calculated from the CD analysis reported previously.
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Acknowledgments
Special thanks should go to Dr. D. Small and the late Dr. M. Walsh for their insightful discussions. This project was partially supported by an award from the National Institutes of Health (NIH).
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Khachfe, H.M., Atkinson, D. Conformation and stability properties of B17: II. Analytical investigations using differential scanning calorimetry. Eur Biophys J 42, 309–314 (2013). https://doi.org/10.1007/s00249-012-0876-7
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DOI: https://doi.org/10.1007/s00249-012-0876-7