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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
52
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pubmed:dateCreated |
2008-12-25
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pubmed:abstractText |
A general strategy for the site-specific dual-labeling of proteins for single-molecule fluorescence resonance energy transfer is presented. A genetically encoded unnatural ketone amino acid was labeled with a hydroxylamine-containing fluorophore with high yield (>95%) and specificity. This methodology was used to construct dual-labeled T4 lysozyme variants, allowing the study of T4 lysozyme folding at single-molecule resolution. The presented strategy is anticipated to expand the scope of single-molecule protein structure and function studies.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-12518054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-15563591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-1591236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-16221762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-16452617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-16857738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-17299036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-17400925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-18221865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-18412538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-18683929,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19108697-3586019
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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 |
Dec
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pubmed:issn |
1520-5126
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
31
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pubmed:volume |
130
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17664-5
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pubmed:dateRevised |
2010-12-17
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pubmed:meshHeading |
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pubmed:year |
2008
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pubmed:articleTitle |
A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer.
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pubmed:affiliation |
Department of Molecular Biology, Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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