Characterization of a reversible denaturational transition occurring in the case of an irreversibly denaturing membrane spanning protein.
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Summary
This reversible thermal transition, manifested by a change in the temperature course of the heat capacity at the protein thermodenaturation temperature, is characterized and briefly discussed.
- Type
- article
- Published
- 1990-02-14
- Cited by
- 0
- References
- 13
- OpenAlex
- https://openalex.org/W2306249
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:45128015
Keywords
Political science
References
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- A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study.
- Theory of large-amplitude conformational fluctuations in native globular proteins. Independent fluctuating site model.
- On the role of reversible denaturation (unfolding) in the irreversible thermal inactivation of enzymes
- Thermodynamics of protein-ligand interactions: calorimetric approaches.
- An Implication of the Structure of Bacteriorhodopsin: Globular Membrane Proteins are Stabilized by Polar Interactions.
- Stability of proteins. Proteins which do not present a single cooperative system.
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