Linear extrapolation method of analyzing solvent denaturation curves

• Published in: Proteins, structure, function, and bioinformatics Vol. 41; no. S4; pp. 1 - 7
• Main Authors: Pace, C. Nick, Shaw, Kevin L.
• Format: Journal Article
• Language: English
• Published: New York John Wiley & Sons, Inc 2000
• Subjects: conformational stability; denatured state; m value; protein folding; urea
• ISSN: 0887-3585; 1097-0134
• DOI: 10.1002/1097-0134(2000)41:4+<1::AID-PROT10>3.0.CO;2-2

The two most common methods of measuring the conformational stability of a protein are differential scanning calorimetry and an analysis of solvent denaturation curves by using the linear extrapolation method. In this article, we trace the history of the linear extrapolation method, review how the method is used to measure protein stability, and then discuss some of the other important uses. Proteins 2000;Suppl 4:1–7. © 2000 Wiley‐Liss, Inc.