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pubmed-article:19140010pubmed:abstractTextSample solubility is essential for structural studies of proteins by solution NMR. Attachment of a solubility enhancement tag, such as GB1, MBP and thioredoxin, to a target protein has been used for this purpose. However, signal overlap of the tag with the target protein often made the spectral analysis difficult. Here we report a sortase-mediated protein ligation method to eliminate NMR signals arising from the tag by preparing the isotopically labeled target protein attached with the non-labeled GB1 tag at the C-terminus.lld:pubmed
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pubmed-article:19140010pubmed:authorpubmed-author:InagakiFuyuhi...lld:pubmed
pubmed-article:19140010pubmed:authorpubmed-author:KumetaHiroyuk...lld:pubmed
pubmed-article:19140010pubmed:authorpubmed-author:KobashigawaYo...lld:pubmed
pubmed-article:19140010pubmed:authorpubmed-author:OguraKenjiKlld:pubmed
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pubmed-article:19140010pubmed:volume43lld:pubmed
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pubmed-article:19140010pubmed:pagination145-50lld:pubmed
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pubmed-article:19140010pubmed:year2009lld:pubmed
pubmed-article:19140010pubmed:articleTitleAttachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method.lld:pubmed
pubmed-article:19140010pubmed:affiliationDepartment of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Hokkaido, 060-0810, Japan.lld:pubmed
pubmed-article:19140010pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19140010pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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