ArticleBiophysical journal2005
Phi-value analysis of a linear, sequential reaction mechanism: theory and application to ion channel gating.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Φ value analysis underscores strong functional and structural compactness of the GABAProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Pathways for nicotinic receptor desensitization.The Journal of general physiology · 2020Article
- The conformational wave in capsaicin activation of transient receptor potential vanilloid 1 ion channel.Nature communications · 2018Article
- 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
- Insights into the gating mechanism of the ryanodine-modified human cardiac Ca2+-release channel (ryanodine receptor 2).Molecular pharmacology · 2014Article
- Agonists binding nicotinic receptors elicit specific channel-opening patterns at αγ and αδ sites.The Journal of physiology · 2014Article
- Conformational changes in acetylcholine binding protein investigated by temperature accelerated molecular dynamics.PloS one · 2014Article
- Hydrophobic interactions between the voltage sensor and pore mediate inactivation in Kv11.1 channels.The Journal of general physiology · 2013Article
- The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013Review
- Pore helices play a dynamic role as integrators of domain motion during Kv11.1 channel inactivation gating.The Journal of biological chemistry · 2013Article
- An outline of desensitization in pentameric ligand-gated ion channel receptors.Cellular and molecular life sciences : CMLS · 2013Review
- Conserved N-terminal negative charges support optimally efficient N-type inactivation of Kv1 channels.PloS one · 2013Article
- Energetic contributions to channel gating of residues in the muscle nicotinic receptor β1 subunit.PloS one · 2013Article
- Functional anatomy of an allosteric protein.Nature communications · 2013Article
- An integrated catch-and-hold mechanism activates nicotinic acetylcholine receptors.The Journal of general physiology · 2012Article
- Sources of energy for gating by neurotransmitters in acetylcholine receptor channels.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The intrinsic energy of the gating isomerization of a neuromuscular acetylcholine receptor channel.The Journal of general physiology · 2012Article
- Design and control of acetylcholine receptor conformational change.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Mapping the sequence of conformational changes underlying selectivity filter gating in the K(v)11.1 potassium channel.Nature structural & molecular biology · 2011Article
Corrections and comments
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- Erratum issued
Authors and funding
3 authors.
Funding
Abstract
We derive the analytical form of a rate-equilibrium free-energy relationship (with slope Phi) for a bounded, linear chain of coupled reactions having arbitrary connecting rate constants. The results confirm previous simulation studies showing that Phi-values reflect the position of the perturbed reaction within the chain, with reactions occurring earlier in the sequence producing higher Phi-values than those occurring later in the sequence. The derivation includes an expression for the transmission coefficients of the overall reaction based on the rate constants of an arbitrary, discrete, finite Markov chain. The results indicate that experimental Phi-values can be used to calculate the relative heights of the energy barriers between intermediate states of the chain but provide no information about the energies of the wells along the reaction path. Application of the equations to the case of diliganded acetylcholine receptor channel gating suggests that the transition-state ensemble for this reaction is nearly flat. Although this mechanism accounts for many of the basic features of diliganded and unliganded acetylcholine receptor channel gating, the experimental rate-equilibrium free-energy relationships appear to be more linear than those predicted by the theory.
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