ArticleProceedings of the National Academy of Sciences of the United States of America2013
Allosteric mechanisms can be distinguished using structural mass spectrometry.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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75 citing papers in PubMed, 151 citations in OpenAlex.
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- Mass Spectrometry- and Structural Biology-Based Investigation of Proteins.Advances in experimental medicine and biology · 2026Review
- Merging different allosteric mechanisms: The case ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- ZnJournal of the American Chemical Society · 2025Article
- Structural basis of nearest-neighbor cooperativity in the ring-shaped gene regulatory protein TRAP from protein engineering and cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein Complex Heterogeneity and Topology Revealed by Electron Capture Charge Reduction and Surface Induced Dissociation.ACS central science · 2024Article
- Protein complex heterogeneity and topology revealed by electron capture charge reduction and surface induced dissociation.bioRxiv : the preprint server for biology · 2024Article
- Low-temperature features of the psychrophilic chaperonin from Pseudoalteromonas haloplanktis.Archives of microbiology · 2024Article
- Structural basis of nearest-neighbor cooperativity in the ring-shaped gene regulatory protein TRAP from protein engineering and cryo-EM.bioRxiv : the preprint server for biology · 2024Article
- Native mass spectrometry analysis of conjugated HSA and BSA complexes with various flavonoids.The Analyst · 2024Article
- Native Capillary Electrophoresis-Mass Spectrometry of Near 1 MDa Non-Covalent GroEL/GroES/Substrate Protein Complexes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time.ACS central science · 2023Article
- Step toward Probing the Nonannular Belt of Membrane Proteins.Analytical chemistry · 2022Article
- Thermodynamic coupling between neighboring binding sites in homo-oligomeric ligand sensing proteins from mass resolved ligand-dependent population distributions.Protein science : a publication of the Protein Society · 2022Article
- Surface Activity of Amines Provides Evidence for the Combined ESI Mechanism of Charge Reduction for Protein Complexes.Analytical chemistry · 2022Article
- Native Mass Spectrometry: Recent Progress and Remaining Challenges.Annual review of biophysics · 2022Review
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- Temperature Regulates Stability, Ligand Binding (MgJournal of the American Chemical Society · 2022Article
- Surface-Induced Dissociation for Protein Complex Characterization.Methods in molecular biology (Clifton, N.J.) · 2022Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity of many proteins, including metabolic enzymes, molecular machines, and ion channels, is often regulated by conformational changes that are induced or stabilized by ligand binding. In cases of multimeric proteins, such allosteric regulation has often been described by the concerted Monod-Wyman-Changeux and sequential Koshland-Némethy-Filmer classic models of cooperativity. Despite the important functional implications of the mechanism of cooperativity, it has been impossible in many cases to distinguish between these various allosteric models using ensemble measurements of ligand binding in bulk protein solutions. Here, we demonstrate that structural MS offers a way to break this impasse by providing the full distribution of ligand-bound states of a protein complex. Given this distribution, it is possible to determine all the binding constants of a ligand to a highly multimeric cooperative system, and thereby infer its allosteric mechanism. Our approach to the dissection of allosteric mechanisms relies on advances in MS--which provide the required resolution of ligand-bound states--and in data analysis. We validated our approach using the well-characterized Escherichia coli chaperone GroEL, a double-heptameric ring containing 14 ATP binding sites, which has become a paradigm for molecular machines. The values of the 14 binding constants of ATP to GroEL were determined, and the ATP-loading pathway of the chaperone was characterized. The methodology and analyses presented here are directly applicable to numerous other cooperative systems and are therefore expected to promote further research on allosteric systems.
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