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Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction
States along the phosphoryl transfer reaction catalyzed by the nucleoside monophosphate kinase UmpK were captured and changes in the conformational heterogeneity of conserved active site arginine side‐chains were quantified by NMR spin‐relaxation methods. In addition to apo and ligand‐bound UmpK, a...
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| Опубликовано в: : | Angew Chem Int Ed Engl |
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| Главные авторы: | , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
John Wiley and Sons Inc.
2016
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5026167/ https://ncbi.nlm.nih.gov/pubmed/27534930 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/anie.201606238 |
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