The catalytic mechanism of an aspartic proteinase explored with neutron and X-ray diffraction.

@article{Coates2008TheCM,
  title={The catalytic mechanism of an aspartic proteinase explored with neutron and X-ray diffraction.},
  author={Leighton Coates and Han-Fang Tuan and Stephen J Tomanicek and Andrey Y Kovalevsky and Marat Mustyakimov and Peter Erskine and Jon D. Cooper},
  journal={Journal of the American Chemical Society},
  year={2008},
  volume={130 23},
  pages={7235-7}
}
Hydrogen atoms play key roles in enzyme mechanism, but as this study shows, even high-quality X-ray data to a resolution of 1 A cannot directly visualize them. Neutron diffraction, however, can locate deuterium atoms even at resolutions around 2 A. Both neutron and X-ray diffraction data have been used to investigate the transition state of the aspartic proteinase endothiapepsin. The different techniques reveal a different part of the story, revealing the clearest picture yet of the catalytic… CONTINUE READING

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nCNS, a patch for CNS

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