ArticleProceedings of the National Academy of Sciences of the United States of America2005
A speed limit for conformational change of an allosteric membrane protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Dimerization mechanism of an inverted-topology ion channel in membranes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Allosteric modulation of α1β3γ2 GABABiophysical journal · 2023Article
- Markov state models of proton- and pore-dependent activation in a pentameric ligand-gated ion channel.eLife · 2021Article
- Unravelling the intricate cooperativity of subunit gating in P2X2 ion channels.Scientific reports · 2020Article
- A novel theoretical framework reveals more than one voltage-sensing pathway in the lateral membrane of outer hair cells.The Journal of general physiology · 2020Article
- Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine.Nature communications · 2019Article
- Autoimmune Channelopathies at Neuromuscular Junction.Frontiers in neurology · 2019Review
- Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions.eLife · 2017Article
- A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip.The Journal of general physiology · 2017Article
- Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol Dehydrogenase.Journal of the American Chemical Society · 2015Article
- Salinity tolerance in plants. Quantitative approach to ion transport starting from halophytes and stepping to genetic and protein engineering for manipulating ion fluxes.Frontiers in plant science · 2015Review
- Quantitative description of ion transport via plasma membrane of yeast and small cells.Frontiers in plant science · 2015Review
- Modeling ion channels: past, present, and future.The Journal of general physiology · 2014Review
- Discovering electrophysiology in photobiology: A brief overview of several photobiological processes with an emphasis on electrophysiology.Communicative & integrative biology · 2014Review
- Seeking structural specificity: direct modulation of pentameric ligand-gated ion channels by alcohols and general anesthetics.Pharmacological reviews · 2014Review
- Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes.Quarterly reviews of biophysics · 2013Review
- The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013Review
- A linkage analysis toolkit for studying allosteric networks in ion channels.The Journal of general physiology · 2013Article
- Identification of a novel post-hydrolytic state in CFTR gating.The Journal of general physiology · 2012Article
- Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.Journal of the American Chemical Society · 2012Article
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Authors and funding
2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Neuromuscular acetylcholine receptors are synaptic ion channels that open and close with rate constants of approximately equal to 48,000 s(-1) and approximately equal to 1,700 s(-1), respectively (in adult mouse, at 24 degrees C, -100 mV membrane potential). Perturbations of many different sites in the protein can change these rate constants, with those in the extracellular domain mainly affecting channel-opening and many of those in the membrane and intracellular domains mainly affecting channel-closing. We used single-channel recordings to measure the total open time per activation (tau(b)) elicited by a low concentration of the natural transmitter, acetylcholine. tau(b) increased in constructs with mutations that increased the gating equilibrium constant by either increasing the opening or decreasing the closing rate constant. However, tau(b) did not approach the same asymptote in fast-opening and slow-closing constructs. The maximum value for the slow closers was about twice that for the fast openers. One interpretation of this difference is that there is an upper limit to the channel-opening rate constant, which we estimate to be approximately 0.86 mus(-1). One possibility is that this limit is the rate of conformational change in the absence of an overall activation barrier and thus reflects the kinetic prefactor for the acetylcholine receptor opening isomerization.
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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.