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Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix
The deer mouse, Peromyscus maniculatus, exhibits altitude-associated variation in hemoglobin oxygen affinity. To examine the structural basis of this functional variation, the structure of the hemoglobin was solved. Recombinant hemoglobin was expressed in Escherichia coli and was purified by ion-exc...
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| Auteurs principaux: | , , , , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
International Union of Crystallography
2013
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3614163/ https://ncbi.nlm.nih.gov/pubmed/23545644 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309113005708 |
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