ArticleBiophysical journal2008
Thermodynamics of activation gating in olfactory-type cyclic nucleotide-gated (CNGA2) channels.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- Voltage vs. Ligand I: Structural basis of the intrinsic flexibility of S3 segment and its significance in ion channel activation.Channels (Austin, Tex.) · 2019Article
- Mechanisms of regulation of olfactory transduction and adaptation in the olfactory cilium.PloS one · 2014Article
- Free-energy relationships in ion channels activated by voltage and ligand.The Journal of general physiology · 2013Article
- Article
- Probability fluxes and transition paths in a Markovian model describing complex subunit cooperativity in HCN2 channels.PLoS computational biology · 2012Article
- Temperature dependence of acetylcholine receptor channels activated by different agonists.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Olfactory-type cyclic nucleotide-gated (CNG) ion channels open by the binding of cyclic nucleotides to a binding domain in the C-terminus. Employing the Eyring rate theory, we performed a thermodynamic analysis of the activation gating in homotetrameric CNGA2 channels. Lowering the temperature shifted the concentration-response relationship to lower concentrations, resulting in a decrease of both the enthalpy DeltaH and entropy DeltaS upon channel opening, suggesting that the order of an open CNGA2 channel plus its environment is higher than that of the closed channel. Activation time courses induced by cGMP concentration jumps were used to study thermodynamics of the transition state. The activation enthalpies DeltaH++ were positive at all cGMP concentrations. In contrast, the activation entropy DeltaS++ was positive at low cGMP concentrations and became then negative at increasing cGMP concentrations. The enthalpic and entropic parts of the activation energies approximately balance each other at all cGMP concentrations, leaving the free enthalpy of activation in the range between 19 and 21 kcal/mol. We conclude that channel activation proceeds through different pathways at different cGMP concentrations. Compared to the unliganded channel, low cGMP concentrations generate a transitional state of lower order whereas high cGMP concentrations generate a transitional state of higher order.
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