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Using Unnatural Amino Acids to Probe the Energetics of Oxyanion Hole Hydrogen Bonds in the Ketosteroid Isomerase Active Site
[Image: see text] Hydrogen bonds are ubiquitous in enzyme active sites, providing binding interactions and stabilizing charge rearrangements on substrate groups over the course of a reaction. But understanding the origin and magnitude of their catalytic contributions relative to hydrogen bonds made...
Tallennettuna:
| Päätekijät: | , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
American Chemical
Society
2014
|
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4046884/ https://ncbi.nlm.nih.gov/pubmed/24787954 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja413174b |
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