Article
Protein stability curves
Article first published online: 1 FEB 2004
DOI: 10.1002/bip.360261104
Copyright © 1987 John Wiley & Sons, Inc.
Additional Information
How to Cite
Becktel, W. J. and Schellman, J. A. (1987), Protein stability curves. Biopolymers, 26: 1859–1877. doi: 10.1002/bip.360261104
Publication History
- Issue published online: 1 FEB 2004
- Article first published online: 1 FEB 2004
- Manuscript Accepted: 21 MAY 1987
- Manuscript Received: 2 FEB 1987
- Abstract
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- Cited By
Abstract
The stability curve of a protein is defined as the plot of the free energy of unfolding as a function of temperature. For most proteins the change in heat capacity on denaturation, or unfolding, is large but approximately constant. When unfolding is s two-state process, most of the salient features of the stability curves of proteins can be derived from this fact. A number of relations are obtained, including the special features of low-temperature denaturation, the properties of the maximum in stability, and the interrelationships of the characteristic temperatures of the protein. The paper closes with a formula that permits one to calculate small changes in stabilization free energy from changes in the melting temperature of the protein.

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