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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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Détails bibliographiques
Auteurs principaux: Inoguchi, Noriko, Oshlo, Jake R., Natarajan, Chandrasekhar, Weber, Roy E., Fago, Angela, Storz, Jay F., Moriyama, Hideaki
Format: Artigo
Langue:Inglês
Publié: International Union of Crystallography 2013
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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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