ArticleBiophysical journal2005
Plasticity of acetylcholine receptor gating motions via rate-energy relationships.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013Review
- Functional anatomy of an allosteric protein.Nature communications · 2013Article
- Temperature dependence of acetylcholine receptor channels activated by different agonists.Biophysical journal · 2011Article
- Conformational plasticity of the influenza A M2 transmembrane helix in lipid bilayers under varying pH, drug binding, and membrane thickness.Biochimica et biophysica acta · 2011Article
- Molecular determinants of coupling between the domain III voltage sensor and pore of a sodium channel.Nature structural & molecular biology · 2010Article
- Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms.The Journal of general physiology · 2009Article
- Unliganded gating of acetylcholine receptor channels.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Structural answers and persistent questions about how nicotinic receptors work.Frontiers in bioscience : a journal and virtual library · 2008Review
- A residue at the cytoplasmic entrance of BK-type channels regulating single-channel opening by its hydrophobicity.Biophysical journal · 2008Article
- Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.Biochimica et biophysica acta · 2007Article
- Conformational dynamics of the alphaM3 transmembrane helix during acetylcholine receptor channel gating.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Like other protein conformational changes, ion channel gating requires the protein to achieve a high-energy transition-state structure. It is not known whether ion channel gating takes place on a broad energy landscape on which many alternative transition state structures are accessible, or on a narrow energy landscape where only a few transition-state structures are possible. To address this question, we measured how rate-equilibrium free energy relationships (REFERs) for di-liganded and unliganded acetylcholine receptor gating vary as a function of the gating equilibrium constant. A large slope for the REFER plot indicates an openlike transition state, whereas a small slope indicates a closedlike transition state. Due to this relationship between REFERs and transition-state structure, the sensitivity of the REFER slope to mutation-induced energetic perturbations allows estimation of the breadth of the energy landscape underlying gating. The relatively large sensitivity of di-liganded REFER slopes to energetic perturbations suggests that the motions underlying di-liganded gating take place on a broad, shallow energy landscape where many alternative transition-state structures are accessible.
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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.