Substitutions in woolly mammoth hemoglobin confer biochemical properties adaptive for cold tolerance

@article{Campbell2010SubstitutionsIW,
  title={Substitutions in woolly mammoth hemoglobin confer biochemical properties adaptive for cold tolerance},
  author={Kevin L. Campbell and Jason Roberts and Laura N. Watson and J{\"o}rg Stetefeld and Angela M Sloan and Anthony V. Signore and Jesse W Howatt and Jeremy R. H. Tame and Nadin Rohland and T J Shen and Jeremy J. Austin and Michael Hofreiter and Chien Ho and Roy E. Weber and Alan Cooper},
  journal={Nature Genetics},
  year={2010},
  volume={42},
  pages={536-540}
}
We have genetically retrieved, resurrected and performed detailed structure-function analyses on authentic woolly mammoth hemoglobin to reveal for the first time both the evolutionary origins and the structural underpinnings of a key adaptive physiochemical trait in an extinct species. Hemoglobin binds and carries O2; however, its ability to offload O2 to respiring cells is hampered at low temperatures, as heme deoxygenation is inherently endothermic (that is, hemoglobin-O2 affinity increases… 
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