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Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function

The mechanism of cooperativity in the human hemoglobin tetramer (a dimer of αβ dimers) has historically been modeled as a simple two-state system in which a low-affinity structural form (T) switches, on ligation, to a high-affinity form (R), yielding a net loss of hydrogen bonds and salt bridges in...

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Bibliografiske detaljer
Udgivet i:Proc Natl Acad Sci U S A
Principais autores: Ackers, Gary K., Dalessio, Paula M., Lew, George H., Daugherty, Margaret A., Holt, Jo M.
Format: Artigo
Sprog:Inglês
Udgivet: National Academy of Sciences 2002
Fag:
Online adgang:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC125012/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12119405/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.152225999
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