title: Determining the conformational stability of a protein using urea denaturation curves.
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.
authors.affiliation: Department of Biology, Grove City College, Grove City, PA, USA.
authors.forename: Kevin L
authors.initials: KL
authors.lastname: Shaw
authors.forename: J Martin
authors.initials: JM
authors.lastname: Scholtz
authors.forename: C Nick
authors.initials: CN
authors.lastname: Pace
authors.forename: Gerald R
authors.initials: GR
authors.lastname: Grimsley
mesh_terms: D002942:Circular Dichroism; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D014508:Urea / Q000737:chemistry*
chemical_list: D011506:Proteins; D014508:Urea