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...
Furkejuvvon:
| Publikašuvnnas: | Proc Natl Acad Sci U S A |
|---|---|
| Váldodahkkit: | , |
| Materiálatiipa: | Artigo |
| Giella: | Inglês |
| Almmustuhtton: |
National Academy of Sciences
1978
|
| Fáttát: | |
| Liŋkkat: | 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 |
| Fáddágilkorat: |
Eai fáddágilkorat, Lasit vuosttaš fáddágilkora!
|