ArticleJournal of the American Society for Mass Spectrometry2015
Effective application of bicelles for conformational analysis of G protein-coupled receptors by hydrogen/deuterium exchange mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Probing protein-lipid interactions by hydrogen/deuterium exchange-mass spectrometry: advances, challenges and future directions.Chemical science · 2026Review
- Deciphering molecular determinants of GPBAR1-Gs protein interactions by HDX-MS and cryo-EM.Scientific reports · 2025Article
- Enhanced Sampling and Tailored Collective Variables Yield Reproducible Free Energy Landscapes of Beta-1 Adrenergic Receptor Activation.Journal of chemical theory and computation · 2025Article
- Intracellular cAMP Signaling Pathway via GBiomedicines · 2023Article
- Hydrogen/deuterium exchange-mass spectrometry of integral membrane proteins in native-like environments: current scenario and the way forward.Essays in biochemistry · 2023Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Structure of a GRK5-Calmodulin Complex Reveals Molecular Mechanism of GRK Activation and Substrate Targeting.Molecular cell · 2021Article
- Article
- Structure and Dynamics of GPCRs in Lipid Membranes: Physical Principles and Experimental Approaches.Molecules (Basel, Switzerland) · 2020Review
- HDX-MS: An Analytical Tool to Capture Protein Motion in Action.Biomedicines · 2020Review
- A glimpse into the molecular mechanism of integral membrane proteins through hydrogen-deuterium exchange mass spectrometry.Protein science : a publication of the Protein Society · 2020Review
- Integrating hydrogen-deuterium exchange mass spectrometry with molecular dynamics simulations to probe lipid-modulated conformational changes in membrane proteins.Nature protocols · 2019Article
- Substrate-induced conformational dynamics of the dopamine transporter.Nature communications · 2019Article
- Assembly of a GPCR-G Protein Complex.Cell · 2019Article
- Hydrogen-deuterium exchange mass spectrometry of membrane proteins in lipid nanodiscs.Chemistry and physics of lipids · 2019Review
- Tracking Higher Order Protein Structure by Hydrogen-Deuterium Exchange Mass Spectrometry.Protein and peptide letters · 2019Review
- Optimized Workflow for Selecting Peptides for HDX-MS Data Analyses.Journal of the American Society for Mass Spectrometry · 2018Article
- Direct protein-lipid interactions shape the conformational landscape of secondary transporters.Nature communications · 2018Article
- Low- q Bicelles Are Mixed Micelles.The journal of physical chemistry letters · 2018Article
- Orthosteric and allosteric action of the C5a receptor antagonists.Nature structural & molecular biology · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
G protein-coupled receptors (GPCRs) have important roles in physiology and pathology, and 40% of drugs currently on the market target GPCRs for the treatment of various diseases. Because of their therapeutic importance, the structural mechanism of GPCR signaling is of great interest in the field of drug discovery. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) is a useful tool for analyzing ligand binding sites, the protein-protein interaction interface, and conformational changes of proteins. However, its application to GPCRs has been limited for various reasons, including the hydrophobic nature of GPCRs and the use of detergents in their preparation. In the present study, we tested the application of bicelles as a means of solubilizing GPCRs for HDX-MS studies. GPCRs (e.g., β2-adrenergic receptor [β2AR], μ-opioid receptor, and protease-activated receptor 1) solubilized in bicelles produced better sequence coverage (greater than 90%) than GPCRs solubilized in n-dodecyl-β-D-maltopyranoside (DDM), suggesting that bicelles are a more effective method of solubilization for HDX-MS studies. The HDX-MS profile of β2AR in bicelles showed that transmembrane domains (TMs) undergo lower deuterium uptake than intracellular or extracellular regions, which is consistent with the fact that the TMs are highly ordered and embedded in bicelles. The overall HDX-MS profiles of β2AR solubilized in bicelles and in DDM were similar except for intracellular loop 3. Interestingly, we detected EX1 kinetics, an important phenomenon in protein dynamics, at the C-terminus of TM6 in β2AR. In conclusion, we suggest the application of bicelles as a useful method for solubilizing GPCRs for conformational analysis by HDX-MS.
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