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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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| Main Authors: | , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
1978
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC411237/ https://ncbi.nlm.nih.gov/pubmed/24215 |
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