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Hydrogen Bonding in the Active Site of Ketosteroid Isomerase: Electronic Inductive Effects and Hydrogen Bond Coupling

Computational studies are performed to analyze the physical properties of hydrogen bonds donated by Tyr16 and Asp103 to a series of substituted phenolate inhibitors bound in the active site of ketosteroid isomerase (KSI). As the solution pK(a) of the phenolate increases, these hydrogen bond distance...

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Hlavní autoři: Hanoian, Philip, Sigala, Paul A., Herschlag, Daniel, Hammes-Schiffer, Sharon
Médium: Artigo
Jazyk:Inglês
Vydáno: 2010
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2996240/
https://ncbi.nlm.nih.gov/pubmed/21049962
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi101428e
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