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An artificial di-iron oxo-protein with phenol oxidase activity

Here we report the de novo design and NMR structure of a four-helical bundle di-iron protein with phenol oxidase activity. The introduction of the cofactor-binding and phenol-binding sites required the incorporation of residues that were detrimental to the free energy of folding of the protein. Suff...

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Hlavní autoři: Faiella, Marina, Andreozzi, Concetta, de Rosales, Rafael Torres Martin, Pavone, Vincenzo, Maglio, Ornella, Nastri, Flavia, DeGrado, William F, Lombardi, Angela
Médium: Artigo
Jazyk:Inglês
Vydáno: 2009
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3808167/
https://ncbi.nlm.nih.gov/pubmed/19915535
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/nchembio.257
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