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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2007-4-25
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pubmed:abstractText |
Tear lipocalin (TL) may stabilize the lipid layer of tears through a molten globule state triggered by low pH. EPR spectroscopy with site-directed spin labeling, revealed the side chain mobility of residues on the G-strand of TL in a molten globule state; the G-strand retains beta-sheet structure. All of the side chains of G-strand residues become more loosely packed, especially residues 96-99. In contrast, the highly mobile side chain of residue 95 on the F-G loop, becomes tightly packed. ANS binding to TL in a molten globule state reestablishes tight packing around side chains that are oriented both inside and outside of the barrel. Unlike RBP and BLG; TL has no disulfide bond between G- and H-strands. It is likely that the central beta-sheet in the molten globule state of lipocalins is stabilized by its interactions with the main alpha-helix, rather than the interstrand disulfide bond.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17434452-10193192,
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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 |
Jun
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
357
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
499-504
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:17434452-Anilino Naphthalenesulfonates,
pubmed-meshheading:17434452-Binding Sites,
pubmed-meshheading:17434452-Carrier Proteins,
pubmed-meshheading:17434452-Lipocalin 1,
pubmed-meshheading:17434452-Models, Chemical,
pubmed-meshheading:17434452-Models, Molecular,
pubmed-meshheading:17434452-Phase Transition,
pubmed-meshheading:17434452-Protein Binding,
pubmed-meshheading:17434452-Protein Conformation,
pubmed-meshheading:17434452-Protein Structure, Tertiary,
pubmed-meshheading:17434452-Spectrometry, Fluorescence,
pubmed-meshheading:17434452-Structure-Activity Relationship,
pubmed-meshheading:17434452-Temperature
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pubmed:year |
2007
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pubmed:articleTitle |
Molten globule state of tear lipocalin: ANS binding restores tertiary interactions.
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pubmed:affiliation |
Department of Pathology, UCLA School of Medicine, Jules Stein Eye Institute, 100 Stein Plaza, Los Angeles, CA 90095, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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