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.
CITATION STYLE
Shaw, K. L., Scholtz, J. M., Pace, C. N., & Grimsley, G. R. (2009). Determining the conformational stability of a protein using urea denaturation curves. Methods in Molecular Biology (Clifton, N.J.), 490, 41–55. https://doi.org/10.1007/978-1-59745-367-7_2
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