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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin
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Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin

机译:有序水分子作为合作二聚体血红蛋白中的关键变构介体

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摘要

One of the most remarkable structural as- ects of Scapharca dimeric hemoglobin is the disruption of a very well-ordered water cluster at the subunit interface upon ligand binding. We have explored the role of these crystallo- raphically observed water molecules by site-directed mu- agenesis and osmotic stress techniques. The isosteric muta- ion of Thr-72 - Val in the interface increases oxygen affinity more than 40-fold with a surprising enhancement of cooperativity.
机译:Scapharca二聚体血红蛋白最显着的结构方面之一是在配体结合后破坏了亚单元界面上秩序井然的水团簇。我们已经通过定点诱变和渗透胁迫技术探索了这些晶体学上观察到的水分子的作用。界面上的Thr-72-Val的等位突变使氧亲和力增加了40倍以上,并且协同性显着提高。

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