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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2007-11-21
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pubmed:abstractText |
ANS is widely used as a probe for locating binding sites of proteins and studying structural changes under various external conditions. However, the nature of ANS-binding sites in proteins and the accompanying changes in fluorescence properties are controversial. We examined the steady-state and time-resolved fluorescence of the ANS-protein complexes for tear lipocalin (TL) and its mutants in order to discern the origin of lifetime components via analysis that included the multiexponential decay and the model-free maximum entropy methods. Fluorescence lifetimes of ANS-TL complexes can be grouped into two species, 14.01-17.42 ns and 2.72-4.37 ns. The log-normal analyses of fluorescence spectral shapes reveal the heterogeneous nature of both long- and short-lifetime species. The constructed time-resolved emission, amplitude (TRES) and area normalized (TRANES), and decay-associated spectra are consistent with a model that includes heterogeneous modes of ANS binding with two separate lifetime components. The two lifetime components are not derived from solvent relaxation, but rather may represent different binding modes.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-10407141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-10423455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-10515687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-10823915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-11106170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-11732894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-12766173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-12876309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-1400345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-1510943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-15461462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-15489503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-16461020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-16730413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-16878982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-19431708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-2025683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-2313585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-4067517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-7648862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-8306712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-8537027,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-8679928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-8761444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-8803875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-9449342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-9660186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-9675263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18028215-9742685
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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:issn |
0031-8655
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1405-14
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
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pubmed:articleTitle |
Characterization of fluorescence of ANS-tear lipocalin complex: evidence for multiple-binding modes.
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pubmed:affiliation |
Department of Pathology, UCLA School of Medicine, Jules Stein Eye Institute, Los Angeles, CA, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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