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Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate
The acylation mechanism of a prototypical serine protease-trypsin and its complete free energy reaction profile have been determined by Born-Oppenheimer ab initio QM/MM molecular dynamics simulations with umbrella sampling.
Tallennettuna:
| Päätekijät: | , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2010
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3213857/ https://ncbi.nlm.nih.gov/pubmed/21116528 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c0cc04112b |
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