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Protein stability curves

Becktel, Wayne J., Schellman, John A.·1987·Biopolymers
DOI 10.1002/bip.360261104
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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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Metadata

Authors
Becktel, W. J., & Schellman, J. A.
Venue
Biopolymers
Publisher
Wiley
Published
1987-11
Volume
26
Issue
11
Pages
1859-1877
ISSN
  • 0006-3525 (ISSN-L)
  • 1097-0282
DOI
10.1002/bip.360261104
OpenAlex
W2078933151
Cited by
1,000
References
0
FWCI
6.34
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Protein stability curves. https://app.cochat.ai/papers/10.1002/bip.360261104
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Becktel, W. J., & Schellman, J. A. (1987). Protein stability curves. Biopolymers. https://doi.org/10.1002/bip.360261104

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.