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In hemoglobin (Hb) Roanne, the aspartate residue α94(G1) is replaced by a glutamic acid. This residue plays a key role in the structural changes affecting the αβ2 contact area during the deoxy- to oxy-state transition in the hemoglobin molecule. Aspartate α94(G1) is involved in several contacts both in the deoxy- and oxy-structures. The most important of those is a hydrogen bond with asparagine...
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