Unit

UNIT 28.4 Determining the Conformational Stability of a Protein from Urea and Thermal Unfolding Curves

  1. Gerald R. Grimsley1,
  2. Saul R. Trevino2,
  3. Richard L. Thurlkill3,
  4. J. Martin Scholtz4

Published Online: 1 FEB 2013

DOI: 10.1002/0471140864.ps2804s71

Current Protocols in Protein Science

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.

Author Information

  1. 1

    Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, Texas

  2. 2

    College of Science and Mathematics, Houston Baptist University, Houston, Texas

  3. 3

    Chemistry and Natural Sciences, University of Louisiana Monroe, Monroe, Louisiana

  4. 4

    Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas

Publication History

  1. Published Online: 1 FEB 2013
  2. Published Print: FEB 2013

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. Curr. Protoc. Protein Sci. 71:28.4.1-28.4.14. © 2013 by John Wiley & Sons, Inc.

Keywords:

  • conformational stability;
  • urea denaturation;
  • thermal denaturation;
  • m-value;
  • protein folding