Structure of Greyhound hemoglobin: origin of high oxygen affinity

Bhatt, V.S.; Zaldívar-López, S.; Harris, D.R.; Couto, C.G.; Wang, P.G.; Palmer, A.F.

doi:10.1107/S0907444911006044

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 7
A water-mediated hydrogen-bond network is uniquely present in GrHb. A group of three variations, αAsp30 in GrHb replacing Glu in HuHb, αGln34 in GrHb replacing Leu in HuHb and βGln125 in GrHb replacing Pro in HuHb, creates a water-mediated hydrogen-bond network at the α₁β₁ interface of GrHb (gray), hence lowering its free energy relative to the R2 state of HuHb (purple).

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 67| Part 5| April 2011| Pages 395-402

doi:10.1107/S0907444911006044

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