Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.

@article{Bourne2004FreezeframeIC,
  title={Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.},
  author={Yves Bourne and Hartmuth C. Kolb and Zoran Radic and K. Barry Sharpless and Palmer Taylor and Pascale Marchot},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 6},
  pages={1449-54}
}
The 1,3-dipolar cycloaddition reaction between unactivated azides and acetylenes proceeds exceedingly slowly at room temperature. However, considerable rate acceleration is observed when this reaction occurs inside the active center gorge of acetylcholinesterase (AChE) between certain azide and acetylene reactants, attached via methylene chains to specific inhibitor moieties selective for the active center and peripheral site of the enzyme. AChE catalyzes the formation of its own inhibitor in a… CONTINUE READING
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