UNIT 28.4 Determining the Conformational Stability of a Protein from Urea and Thermal Unfolding Curves
Published Online: 1 FEB 2013
Copyright © 2013 by John Wiley & Sons, Inc.
Lab Protocol Title
Current Protocols in Protein Science
How to Cite
Grimsley, G. R., Trevino, S. R., Thurlkill, R. L. and Scholtz, J. M. 2013. Determining the Conformational Stability of a Protein from Urea and Thermal Unfolding Curves. Current Protocols in Protein Science. 71:28.4:28.4.1–28.4.14.
- Published Online: 1 FEB 2013
- Published Print: FEB 2013
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. Curr. Protoc. Protein Sci. 71:28.4.1-28.4.14. © 2013 by John Wiley & Sons, Inc.
- conformational stability;
- urea denaturation;
- thermal denaturation;
- protein folding