ArticleBiochemistry2012
An outer membrane protein undergoes enthalpy- and entropy-driven transitions.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Understanding Drug Permeability inLife (Basel, Switzerland) · 2025Review
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Article
- Understanding antibiotic resistance via outer membrane permeability.Infection and drug resistance · 2018Review
- Exploring bacterial outer membrane barrier to combat bad bugs.Infection and drug resistance · 2017Review
- The Transmembrane Domain of a Bicomponent ABC Transporter Exhibits Channel-Forming Activity.ACS chemical biology · 2016Article
- Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016Article
- Quasithermodynamic contributions to the fluctuations of a protein nanopore.ACS chemical biology · 2015Article
- Phase coexistence in single-lipid membranes induced by buffering agents.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- Watching single proteins using engineered nanopores.Protein and peptide letters · 2014Review
- Does the lipid environment impact the open-state conductance of an engineered β-barrel protein nanopore?Biochimica et biophysica acta · 2013Article
- Entropy-enthalpy Compensation of Biomolecular Systems in Aqueous Phase: a Dry Perspective.Monatshefte fur chemie · 2013Article
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- Cation selectivity is a conserved feature in the OccD subfamily of Pseudomonas aeruginosa.Biochimica et biophysica acta · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
β-Barrel membrane proteins often fluctuate among various open substates, yet the nature of these transitions is not fully understood. Using temperature-dependent, single-molecule electrophysiology analysis, along with rational protein design, we show that OccK1, a member of the outer membrane carboxylate channel from Pseudomonas aeruginosa, features a discrete gating dynamics comprising both enthalpy-driven and entropy-driven current transitions. OccK1 was chosen for the analysis of these transitions, because it is a monomeric transmembrane β-barrel of a known high-resolution crystal structure and displays three distinguishable, time-resolvable open substates. Native and loop-deletion OccK1 proteins showed substantial changes in the activation enthalpies and entropies of the channel transitions, but modest alterations in the equilibrium free energies, confirming that the system never departs from equilibrium. Moreover, some current fluctuations of OccK1 indicated a counterintuitive, negative activation enthalpy, which was compensated by a significant decrease in the activation entropy. Temperature scanning of the single-channel properties of OccK1 exhibited a thermally induced switch of the energetically most favorable open substate at the lowest examined temperature of 4 °C. Therefore, such a semiquantitative assessment of the current fluctuation dynamics not only demonstrates the complexity of channel gating but also reveals distinct functional traits of a β-barrel outer membrane protein under different temperature circumstances.
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