|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0023690,
umls-concept:C0025663,
umls-concept:C0033684,
umls-concept:C0037293,
umls-concept:C0037628,
umls-concept:C0181496,
umls-concept:C0185023,
umls-concept:C0237497,
umls-concept:C1314972,
umls-concept:C1522485,
umls-concept:C1627358,
umls-concept:C1947904,
umls-concept:C1999228,
umls-concept:C2349975,
umls-concept:C2825781
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|
pubmed:issue |
3
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pubmed:dateCreated |
2009-2-24
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|
pubmed:abstractText |
Sample 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1573-5001
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pubmed:author |
|
|
pubmed:issnType |
Electronic
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
145-50
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pubmed:meshHeading |
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pubmed:year |
2009
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pubmed:articleTitle |
Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method.
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pubmed:affiliation |
Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Hokkaido, 060-0810, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
