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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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Detalhes bibliográficos
Main Authors: Mikulski, Rose, Domsic, John F., Ling, George, Tu, Chingkuang, Robbins, Arthur H., Silverman, David N., McKenna, Robert
Formato: Artigo
Idioma:Inglês
Publicado em: 2011
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Acesso em linha: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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