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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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
2002
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| Assuntos: | |
| Acesso em linha: | 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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