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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 β-sheet structure. All of the side chains of G-strand residues become more loosely packed, especially residues 96–99. In contrast,...
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