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Ground State Destabilization From a Positioned General Base in the Ketosteroid Isomerase Active Site
We compared the binding affinities of ground state analogs for bacterial ketosteroid isomerase (KSI) with a wild-type anionic Asp general base and with uncharged Asn and Ala in the general base position to provide a measure of potential ground state destabilization that could arise from the close ju...
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| Hoofdauteurs: | , , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2013
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3651043/ https://ncbi.nlm.nih.gov/pubmed/23311398 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi301348x |
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