title: Determining the conformational stability of a protein from urea and thermal unfolding curves.
abstract: This unit contains basic protocols for determining the conformational stability of a globular protein from either urea or thermal unfolding curves. Circular dichroism is the optical spectroscopic technique most commonly used to monitor protein unfolding. The protocols describe how to analyze data from an unfolding curve to obtain the thermodynamic parameters necessary to calculate conformational stability, and how to determine differences in stability between protein variants.
authors: Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, Texas, USA.
authors: Gerald R
authors: GR
authors: Grimsley
authors: Saul R
authors: SR
authors: Trevino
authors: Richard L
authors: RL
authors: Thurlkill
authors: J Martin
authors: JM
authors: Scholtz
mesh_terms: D000465:Algorithms; D002942:Circular Dichroism; D011489:Protein Denaturation; D055550:Protein Stability; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics; D014508:Urea / Q000737:chemistry*
chemical_list: D011506:Proteins; D014508:Urea