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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Hlavní autoři: Andersen, Øivind, De Rosa, Maria Cristina, Yadav, Prakash, Pirolli, Davide, Fernandes, Jorge MO, Berg, Paul R, Jentoft, Sissel, Andrè, Carl
Médium: Artigo
Jazyk:Inglês
Vydáno: BioMed Central 2014
Témata:
Research Article
On-line přístup: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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