ArticleJournal of the American Chemical Society2011
Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 95 citations in OpenAlex.
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
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- Scalable production of monovalent streptavidin with high yield and purity.Scientific reports · 2026Article
- Membrane insertion and dimerization of glycophorin-A mutations studied by free energy simulations.Biophysical journal · 2026Article
- Single-molecule tweezers decode hidden dimerization patterns of membrane proteins within lipid bilayers.Nature communications · 2025Article
- The lipid bilayer strengthens the cooperative network of membrane proteins.Science advances · 2025Article
- Lipid unsaturation promotes BAX and BAK pore activity during apoptosis.Nature communications · 2024Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- A Rigorous Framework for Calculating Protein-Protein Binding Affinities in Membranes.Journal of chemical theory and computation · 2023Article
- Comparison of Integrin αIIbβ3 Transmembrane Association in Vesicles and Bicelles.Biochemistry · 2023Article
- Thermodynamic analysis of the GASBiophysical journal · 2023Article
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Untangling the complexity of membrane protein folding.Current opinion in structural biology · 2022Review
- Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Hydrophobic mismatch and sequence specificity compete when transmembrane helix-helix interactions are measured with the TOXCAT assay.Frontiers in chemistry · 2022Article
- Spiers Memorial Lecture: Analysis andFaraday discussions · 2021Article
- The Role of the Membrane in Transporter Folding and Activity.Journal of molecular biology · 2021Review
- Membrane proteins enter the fold.Current opinion in structural biology · 2021Review
- How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020Review
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Membrane proteins have evolved to fold and function in a lipid bilayer, so it is generally assumed that their stability should be optimized in a natural membrane environment. Yet optimal stability is not always in accord with optimization of function, so evolutionary pressure, occurring in a complex membrane environment, may favor marginal stability. Here, we find that the transmembrane helix dimer, glycophorin A (GpATM), is actually much less stable in the heterogeneous environment of a natural membrane than it is in model membranes and even common detergents. The primary destabilizing factors are electrostatic interactions between charged lipids and charged GpATM side chains, and nonspecific competition from other membrane proteins. These effects overwhelm stabilizing contributions from lateral packing pressure and excluded volume. Our work illustrates how evolution can employ membrane composition to modulate protein stability.
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