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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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Argitaratua izan da:Proc Natl Acad Sci U S A
Egile Nagusiak: Valdes, Roland, Ackers, Gary K.
Formatua: Artigo
Hizkuntza:Inglês
Argitaratua: National Academy of Sciences 1978
Gaiak:
Sarrera elektronikoa: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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