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Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole
The catalytic importance of enzyme active-site interactions is frequently assessed by mutating specific residues and measuring the resulting rate reductions. This approach has been used in bacterial ketosteroid isomerase to probe the energetic importance of active-site hydrogen bonds donated to the...
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| Hauptverfasser: | , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
National Academy of Sciences
2010
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2836627/ https://ncbi.nlm.nih.gov/pubmed/20080683 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0911168107 |
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