Self-association of hemoglobin β(SH) chains is linked to oxygenation
Self-association of unliganded β(SH) chains into tetramers (4 β(1) [unk] β(4)) is experimentally found to be energetically less favorable (ΔG(0) = -19.05 ± 0.30 kcal) than the corresponding oligomerization of fully oxygenated chains (4 β(1)X [unk] β(4)X(4); ΔG(0) = -22.45 ± 0.35 kcal). Hence the tet...
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| Udgivet i: | Proc Natl Acad Sci U S A |
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| Principais autores: | , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
National Academy of Sciences
1978
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC411237/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/24215/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.75.1.311 |
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