SpringerProtocols: Abstract: Determining the Conformational Stability of a Protein Using Urea Denaturation Curves

2. Determining the Conformational Stability of a Protein Using Urea Denaturation Curves

By: Kevin L. Shaw², J. Martin Scholtz³, C. Nick Pace³, R. Gerald Grimsley⁴

Abstract

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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.

Affiliation(s): (2) Department of Biology, Grove City College, Grove City, PA, USA
(3) Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, and Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA
(4) Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, Grove City College, College Station, TX, USA

Book Title: Protein Structure, Stability, and Interactions

Series: Methods in Molecular Biology | Volume: 490 | Pub. Date: Mar-01-2008 | Page Range: 1-15 | DOI: 10.1007/978-1-59745-367-7_2

Subject: Protein Science

Key Words: conformational stability - urea denaturation - circular dichroism - fluorescence - UV absorbance spectroscopy

References

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