ArticleBiochemistry2009
Intracavitary ligand distribution in tear lipocalin by site-directed tryptophan fluorescence.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- Tear Lipocalin and Lipocalin-Interacting Membrane Receptor.Frontiers in physiology · 2021Article
- Data on Orphan tear lipid analogs, synthesis and binding to tear lipocalin.Data in brief · 2018Article
- Interaction of ceramides and tear lipocalin.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2018Article
- Double tryptophan exciton probe to gauge proximal side chains in proteins: augmentation at low temperature.The journal of physical chemistry. B · 2015Article
- Antibacterial activity of rifamycins for M. smegmatis with comparison of oxidation and binding to tear lipocalin.Biochimica et biophysica acta · 2014Article
- A simple model-free method for direct assessment of fluorescent ligand binding by linear spectral summation.Journal of fluorescence · 2014Article
- Siderocalins: Siderophore binding proteins evolved for primary pathogen host defense.Current opinion in chemical biology · 2013Review
- Wax-tear and meibum protein, wax-β-carotene interactions in vitro using infrared spectroscopy.Experimental eye research · 2012Article
- Cation-π interactions in lipocalins: structural and functional implications.Biochemistry · 2012Article
- Tear lipocalin: structure and function.The ocular surface · 2011Review
- The conserved disulfide bond of human tear lipocalin modulates conformation and lipid binding in a ligand selective manner.Biochimica et biophysica acta · 2011Article
- Focus on molecules: tear lipocalin.Experimental eye research · 2011Review
- The international workshop on meibomian gland dysfunction: report of the subcommittee on tear film lipids and lipid-protein interactions in health and disease.Investigative ophthalmology & visual science · 2011Review
- Excited protein states of human tear lipocalin for low- and high-affinity ligand binding revealed by functional AB loop motion.Biophysical chemistry · 2010Article
- Tear lipocalin captures exogenous lipid from abnormal corneal surfaces.Investigative ophthalmology & visual science · 2010Article
- pH-Dependent conformational changes in tear lipocalin by site-directed tryptophan fluorescence.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Site-directed tryptophan fluorescence has been successfully used to determine the solution structure of tear lipocalin. Here, the technique is extended to measure the binding energy landscape. Single Trp mutants of tear lipocalin are bound to the native ligand and an analogue tagged with a quencher group to both populate and discriminate the excited protein states. Steady-state and time-resolved fluorescence quenching data reveal the intracavitary state of the ligand. The static components of fluorescence quenching identify the residues where nonfluorescence complexes form. An asymmetric distribution of the ligand within the cavity reflects the complex energy landscape of the excited protein states. These findings suggest that the excited protein states are not unique but consist of many substates. The roughness of the binding energy landscape is about 2.5kBT. The excited protein states originate primarily from conformational selections of loops AB and GH, a portal region. In contrast to static quenching, the dynamic components of fluorescence quenching by the ligand are relevant to both local side chain and ligand dynamics. Apparent bimolecular rate constants for collisional quenching of Trp by the nitroxide moiety are approximately 1 / 5 x 10(12) M(-1) s(-1). Estimations made for effective ligand concentrations establish actual rate constants on the order of 12 x 10(9) M(-1) s(-1). Prior to exit from the cavity of the protein, ligands explore binding sites in nanoseconds. Although microsecond fluctuations are rate-limiting processes in ligand binding for many proteins, accompanying nanosecond motion may be necessary for propagation of ligand binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.