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...

Täydet tiedot

Bibliografiset tiedot

Julkaisussa:	Proc Natl Acad Sci U S A
Päätekijät:	Valdes, Roland, Ackers, Gary K.
Aineistotyyppi:	Artigo
Kieli:	Inglês
Julkaistu:	National Academy of Sciences 1978
Aiheet:	Biological Sciences: Biophysics
Linkit:	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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