Abstract
The stability of globular proteins is an important factor in determining their usefulness in basic research and medicine. A number of environmental factors contribute to the conformational stability of a protein, including pH, temperature, and ionic strength. In addition, variants of proteins may show remarkable differences in stability from their wild-type form. In this chapter, we describe the method and analysis of urea denaturation curves to determine the conformational stability of a protein. This involves relatively simple experiments that can be done in a typical biochemistry laboratory, especially when using ordinary spectroscopic techniques to follow unfolding.
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Shaw, K.L., Scholtz, J.M., Pace, C.N., Grimsley, R.G. (2009). Determining the Conformational Stability of a Protein Using Urea Denaturation Curves. 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_2
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DOI: https://doi.org/10.1007/978-1-59745-367-7_2
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