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Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

The transition state for the R in equilibrium with T quaternary conformational change of hemoglobin has thermodynamic properties much closer to those of the R conformation than to those of the T conformation. This finding is based on a comparison of activation and equilibrium enthalpy and entropy ch...

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Détails bibliographiques
Publié dans:Proc Natl Acad Sci U S A
Auteurs principaux: Eaton, W A, Henry, E R, Hofrichter, J
Format: Artigo
Langue:Inglês
Publié: National Academy of Sciences 1991
Sujets:
Accès en ligne:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC51682/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2034685/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.88.10.4472
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