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...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1991
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| Témata: | |
| On-line přístup: | 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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