Journal article
Determining the conformational stability of a protein using urea denaturation curves
Methods in molecular biology (Clifton, N.J.), Vol.490, pp.41-55
2009
DOI: 10.1007/978-1-59745-367-7_2
PMID: 19157078
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.
Details
- Title: Subtitle
- Determining the conformational stability of a protein using urea denaturation curves
- Creators
- Kevin L Shaw - Grove City CollegeJ Martin Scholtz - Mitchell InstituteC Nick Pace - Mitchell InstituteGerald R Grimsley
- Resource Type
- Journal article
- Publication Details
- Methods in molecular biology (Clifton, N.J.), Vol.490, pp.41-55
- DOI
- 10.1007/978-1-59745-367-7_2
- PMID
- 19157078
- eISBN
- 9781597453677; 1597453676
- ISSN
- 1064-3745
- eISSN
- 1940-6029
- Language
- English
- Date published
- 2009
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984288727402771
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