Abstract
Ultrasensitive microcalorimetric techniques for measuring the heat capacities of proteins in dilute solutions over a broad temperature range (DSC) and the heats of protein reactions at fixed temperatures (ITC) are described and the methods of working with these instruments are considered. Particular attention is paid to analyzing the thermal properties of individual proteins, their stability, the energetics of their folding, and their association with specific macromolecular partners. Use of these calorimetric methods is illustrated with examples of small compact globular proteins, small proteins having loose noncompact structure, multidomain proteins, and protein complexes, particularly with DNA.
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Acknowledgments
The author would like to thank Dr. Colyn Crane-Robinson for a critical reading of the text and Dr. Anatoly Dragan for assistance in preparing illustrations. The financial support of NSF Grant MCB 0519381 is acknowledged.
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Privalov, P.L. (2009). Microcalorimetry of Proteins and Their Complexes. In: Shriver, J. (eds) Protein Structure, Stability, and Interactions. Methods in Molecular Biology, vol 490. Humana Press. https://doi.org/10.1007/978-1-59745-367-7_1
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DOI: https://doi.org/10.1007/978-1-59745-367-7_1
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