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Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state

With more than 500 crystal structures determined, serine proteases make up greater than one-third of all proteases structurally examined to date, making them among the best biochemically and structurally characterized enzymes. Despite the numerous crystallographic and biochemical studies of trypsin...

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Autors principals: Blankenship, Elise, Vukoti, Krishna, Miyagi, Masaru, Lodowski, David T.
Format: Artigo
Idioma:Inglês
Publicat: International Union of Crystallography 2014
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC3949523/
https://ncbi.nlm.nih.gov/pubmed/24598752
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1399004713033658
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