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Thermodynamics of ubiquitin unfolding

Wintrode, Patrick L., Makhatadze, George I., Privalov, Peter L.·1994·Proteins: Structure, Function, and Bioinformatics

Abstract

The energetics of ubiquitin unfolding have been studied using differential scanning microcalorimetry. For the first time it has been shown directly that the enthalpy of protein unfolding is a nonlinear function of temperature. Thermodynamic parameters of ubiquitin unfolding were correlated with the structure of the protein. The enthalpy of hydrogen bonding in ubiquitin was calculated and compared to that obtained for other proteins. It appears that the energy of hydrogen bonding correlates with the average length of the hydrogen bond in a given protein structure. © 1994 John Wiley & Sons, Inc.

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Metadata

Authors
Wintrode, P. L., Makhatadze, G. I., & Privalov, P. L.
Venue
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley
Published
1994-03
Volume
18
Issue
3
Pages
246-253
ISSN
  • 0887-3585 (ISSN-L)
  • 1097-0134
OpenAlex
W2122680286
Cited by
185
References
0
FWCI
2.08
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Thermodynamics of ubiquitin unfolding. https://app.cochat.ai/papers/10.1002/prot.340180305
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Wintrode, P. L., Makhatadze, G. I., & Privalov, P. L. (1994). Thermodynamics of ubiquitin unfolding. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.340180305

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