ArticleJournal of the American Society for Mass Spectrometry2003
Indirect assessment of small hydrophobic ligand binding to a model protein using a combination of ESI MS and HDX/ESI MS.
Article in Journal of the American Society for Mass Spectrometry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 40 citations in OpenAlex.
- Probing protein-lipid interactions by hydrogen/deuterium exchange-mass spectrometry: advances, challenges and future directions.Chemical science · 2026Review
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- Organic Solvents for Enhanced Proteolysis of Stable Proteins for Hydrogen-Deuterium Exchange Mass Spectrometry.Analytical chemistry · 2020Article
- Evolution of Structural Biology through the Lens of Mass Spectrometry.Analytical chemistry · 2019Review
- Kinetics of Protein Complex Dissociation Studied by Hydrogen/Deuterium Exchange and Mass Spectrometry.Analytical chemistry · 2015Article
- QUDeX-MS: hydrogen/deuterium exchange calculation for mass spectra with resolved isotopic fine structure.BMC bioinformatics · 2014Article
- Hydrogen exchange mass spectrometry: are we out of the quicksand?Journal of the American Society for Mass Spectrometry · 2012Review
- Transferrin as a model system for method development to study structure, dynamics and interactions of metalloproteins using mass spectrometry.Biochimica et biophysica acta · 2012Review
- Comparison of Two ESI MS Based H/D Exchange Methods for Extracting Protein Folding Energies.International journal of mass spectrometry · 2009Article
- H/D exchange and mass spectrometry in the studies of protein conformation and dynamics: is there a need for a top-down approach?Analytical chemistry · 2009Article
- Article
- Transient structural disorder as a facilitator of protein-ligand binding: native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I.Journal of the American Society for Mass Spectrometry · 2005Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Direct mass spectrometric characterization of interactions between proteins and small hydrophobic ligands often poses a serious problem due to the complex instability in the gas phase. We have developed a method that probes the efficacy of ligand-protein interactions indirectly by monitoring changes in protein flexibility. The latter is assessed quantitatively using a combination of charge state distribution analysis and amide hydrogen exchange under both native and mildly denaturing conditions. The method was used to evaluate binding of a model protein cellular retinoic acid binding protein I to its natural ligand all-trans retinoic acid (RA), isomers 13-cis- and 9-cis-RA, and retinol, yielding the following order of ligand affinities: All-trans RA > 9-cis RA > 13-cis RA, with no detectable binding of retinol. This order is in agreement with the results of earlier fluorimetric titration studies. Furthermore, binding energy of the protein to each of retinoic acid isomers was determined based on the measured hydrogen exchange kinetics data acquired under native conditions.
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