ArticleProceedings of the National Academy of Sciences of the United States of America2023
A thermodynamic analysis of CLC transporter dimerization in lipid bilayers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 7 citations in OpenAlex.
- Quantitative and amino acid sequence analysis of soluble HIV-1 Vpu and calmodulin interactions.Protein science : a publication of the Protein Society · 2026Article
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
- When membrane proteins prefer lipids.Nature chemical biology · 2026Article
- Molecular basis for the regulation of membrane proteins through preferential lipid solvation.Nature chemical biology · 2026Article
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026Article
- A roadmap to cysteine specific labeling of membrane proteins for single-molecule photobleaching studies.Methods (San Diego, Calif.) · 2025Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Dimerization mechanism of an inverted-topology ion channel in membranes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Membrane defects as a generalized driving force for membrane protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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7 authors at 4 institutions in 1 country.
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Abstract
The CLC-ec1 chloride/proton antiporter is a membrane-embedded homodimer with subunits that can dissociate and associate, but the thermodynamic driving forces favor the assembled dimer at biological densities. Yet, the physical reasons for this stability are confounding as dimerization occurs via the burial of hydrophobic interfaces away from the lipid solvent. For binding of nonpolar surfaces in aqueous solution, the driving force is often attributed to the hydrophobic effect, but this should not apply in the membrane since there is very little water. To investigate this further, we quantified the thermodynamic changes associated with CLC dimerization in membranes by carrying out a van 't Hoff analysis of the temperature dependency of the free energy of dimerization, Δ
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