ArticleBiochemistry2010
pH-Dependent conformational changes in tear lipocalin by site-directed tryptophan fluorescence.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Physicochemical properties of amyloid-like fibrils from ultrasonication-induced plum seed protein-catechin conjugates.Food chemistry: X · 2026Article
- Effects of ligand binding on dynamics of fatty acid binding protein and interactions with membranes.Biophysical journal · 2022Article
- Mutation in the CX3C Motif of G Protein Disrupts Its Interaction with Heparan Sulfate: A Calorimetric, Spectroscopic, and Molecular Docking Study.International journal of molecular sciences · 2022Article
- Article
- Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions.Molecules (Basel, Switzerland) · 2021Article
- Tear Lipocalin and Lipocalin-Interacting Membrane Receptor.Frontiers in physiology · 2021Article
- Probing of carotenoid-tryptophan hydrogen bonding dynamics in the single-tryptophan photoactive Orange Carotenoid Protein.Scientific reports · 2020Article
- A conformation-specific ON-switch for controlling CAR T cells with an orally available drug.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Double tryptophan exciton probe to gauge proximal side chains in proteins: augmentation at low temperature.The journal of physical chemistry. B · 2015Article
- Exploring protein solution structure: Second moments of fluorescent spectra report heterogeneity of tryptophan rotamers.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2015Article
- Probing tertiary structure of proteins using single Trp mutations with circular dichroism at low temperature.The journal of physical chemistry. B · 2014Article
- Article
- Tryptophan rotamer distribution revealed for the α-helix in tear lipocalin by site-directed tryptophan fluorescence.The journal of physical chemistry. B · 2012Article
- Cation-π interactions in lipocalins: structural and functional implications.Biochemistry · 2012Article
- The conserved disulfide bond of human tear lipocalin modulates conformation and lipid binding in a ligand selective manner.Biochimica et biophysica acta · 2011Article
- Excited protein states of human tear lipocalin for low- and high-affinity ligand binding revealed by functional AB loop motion.Biophysical chemistry · 2010Article
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Authors and funding
3 authors.
Funding
Abstract
Tear lipocalin (TL), a major protein of human tears, binds a broad array of endogenous ligands. pH-dependent ligand binding in TL may have functional implications in tears. Previously, conformational selections of the AB and GH loops have been implicated in ligand binding by site-directed tryptophan fluorescence (SDTF). In this study, SDTF was applied to the AB and GH loops to investigate pH-driven conformational changes relevant to ligand binding. Both loops demonstrate significant but distinct conformational rearrangements over a wide pH range. In the low-pH transition, from 7.3 to 3.0, residues of the GH loop exhibit decreased solvent accessibilities. In acrylamide quenching experiments, the average quenching rate constant (k(q), accessibility parameter) of the residues in the GH loop is decreased approximately 38%, from 2.1 x 10(9) to 1.3 x 10(9) M(-1) s(-1). However, despite the significant changes in accessibilities for some residues in the AB loop, the average accessibility per residue remained unchanged (average k(q) = 1.2 M(-1) s(-1)). Accordingly, the low-pH transition induces conformational changes that reshuffle the accessibility profiles of the residues in the AB loop. A significant difference in the titration curves between the holo and apo forms of the W28 mutant suggests that the protonation states of the residues around position 28 modulate conformational switches of the AB loop relevant to ligand binding.
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