| pubmed-article:17434452 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17434452 | lifeskim:mentions | umls-concept:C0004388 | lld:lifeskim |
| pubmed-article:17434452 | lifeskim:mentions | umls-concept:C0078147 | lld:lifeskim |
| pubmed-article:17434452 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:17434452 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:17434452 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:17434452 | lifeskim:mentions | umls-concept:C1337528 | lld:lifeskim |
| pubmed-article:17434452 | lifeskim:mentions | umls-concept:C0205372 | lld:lifeskim |
| pubmed-article:17434452 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17434452 | pubmed:dateCreated | 2007-4-25 | lld:pubmed |
| pubmed-article:17434452 | 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. | lld:pubmed |
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| pubmed-article:17434452 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17434452 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17434452 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17434452 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17434452 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:17434452 | pubmed:author | pubmed-author:GasymovOktay... | lld:pubmed |
| pubmed-article:17434452 | pubmed:author | pubmed-author:AbduragimovAd... | lld:pubmed |
| pubmed-article:17434452 | pubmed:author | pubmed-author:GlasgowBen... | lld:pubmed |
| pubmed-article:17434452 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17434452 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17434452 | pubmed:volume | 357 | lld:pubmed |
| pubmed-article:17434452 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17434452 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17434452 | pubmed:pagination | 499-504 | lld:pubmed |
| pubmed-article:17434452 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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| pubmed-article:17434452 | pubmed:meshHeading | pubmed-meshheading:17434452... | lld:pubmed |
| pubmed-article:17434452 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17434452 | pubmed:articleTitle | Molten globule state of tear lipocalin: ANS binding restores tertiary interactions. | lld:pubmed |
| pubmed-article:17434452 | pubmed:affiliation | Department of Pathology, UCLA School of Medicine, Jules Stein Eye Institute, 100 Stein Plaza, Los Angeles, CA 90095, USA. | lld:pubmed |
| pubmed-article:17434452 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17434452 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17434452 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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