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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Detaylı Bibliyografya
Asıl Yazarlar: Inoguchi, Noriko, Oshlo, Jake R., Natarajan, Chandrasekhar, Weber, Roy E., Fago, Angela, Storz, Jay F., Moriyama, Hideaki
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: International Union of Crystallography 2013
Konular:
Structural Communications
Online Erişim: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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