The conserved Phe GH5 of importance for hemoglobin intersubunit contact is mutated in gadoid fish

BACKGROUND: Functionality of the tetrameric hemoglobin molecule seems to be determined by a few amino acids located in key positions. Oxygen binding encompasses structural changes at the interfaces between the α1β2 and α2β1 dimers, but also subunit interactions are important for the oxygen binding a...

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Main Authors: Andersen, Øivind, De Rosa, Maria Cristina, Yadav, Prakash, Pirolli, Davide, Fernandes, Jorge MO, Berg, Paul R, Jentoft, Sissel, Andrè, Carl
Formato: Artigo
Idioma:Inglês
Publicado: BioMed Central 2014
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Research Article
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3998052/
https://ncbi.nlm.nih.gov/pubmed/24655798
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1471-2148-14-54
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