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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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Autors principals: Kraut, Daniel A., Sigala, Paul A., Fenn, Timothy D., Herschlag, Daniel
Format: Artigo
Idioma:Inglês
Publicat: National Academy of Sciences 2010
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Accés en línia: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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