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Structure and Catalysis by Carbonic Anhydrase II: Role of Active-Site Tryptophan 5
The tryptophan residue Trp5, highly conserved in the α class of carbonic anhydrases including human carbonic anhydrase II (HCA II), is positioned at the entrance of the active site cavity and forms a π-stacking interaction with the imidazole ring of the proton shuttle His64 in its outward orientatio...
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| Главные авторы: | , , , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2011
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3223279/ https://ncbi.nlm.nih.gov/pubmed/22001224 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.abb.2011.09.011 |
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