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. Author manuscript; available in PMC: 2016 Feb 5.
Published in final edited form as: Biophys Chem. 2007 Feb 16;127(3):181–193. doi: 10.1016/j.bpc.2007.02.002

Figure 10.

Figure 10

The α1β2 interface. The α1β2 interface is depicted, with the α104 Cys highlighted in light pink, and the β93 Cys highlighted in dark pink. The residues forming intersubunit H-bonds (α42 Tyr and β99 Asp) and (β37 Trp and α94 Asp) are highlighted in green and blue respectively. The β85 Phe and β88 Leu residues of the 1β1-2β2 donor-acceptor interaction are shown in purple. Heme groups and coordinating His residues are shown in dark red. The Cα-Cα distance from the α104 Cys to the α42 Tyr (16.6 Å) is shown in green. Diagram was made using WebLab ViewerPro and the coordinates from the deoxy Hb S X-ray crystal structure (2HBS.PDB).