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Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution

In enzyme catalysis, where exquisitely positioned functionality is the sine qua non, atomic coordinates for a Michaelis complex can provide powerful insights into activation of the substrate. We focus here on the initial proton transfer of the isomerization reaction catalyzed by triosephosphate isom...

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Detalhes bibliográficos
Main Authors: Jogl, Gerwald, Rozovsky, Sharon, McDermott, Ann E., Tong, Liang
Formato: Artigo
Idioma:Inglês
Publicado em: The National Academy of Sciences 2003
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC140880/
https://ncbi.nlm.nih.gov/pubmed/12509510
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0233793100
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