ArticleBiochimica et biophysica acta2012
Hydrogen-bond energetics drive helix formation in membrane interfaces.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Membrane-Traversing Peptides: Mechanistic Landscapes, Assays, and Applications.Chemical reviews · 2026Review
- Is the Bilayer Insertion of the Peptide KALP23 Under Kinetic or Thermodynamic Control?The Journal of membrane biology · 2026Article
- Understanding cell-penetrating peptide mechanisms using computational electrophysiology simulations.Protein science : a publication of the Protein Society · 2026Article
- Spatially regulated mRNA translation enables functional membrane protein integration in synthetic cells.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Biological Properties of Arginine-rich Peptides and their Application in Cargo Delivery to Cancer.Current drug delivery · 2025Review
- A molecular dynamics study of cell-penetrating peptide transportan-10 (TP10): Binding, folding and insertion to transmembrane state in zwitterionic membrane.Biochimica et biophysica acta. Biomembranes · 2024Article
- Modeling the Effect on a Novel Fungal Peptaibol Placed in an All-Atom Bacterial Membrane Mimicking System via Accelerated Molecular Dynamics Simulations.Life (Basel, Switzerland) · 2023Article
- Structural flexibility of apolipoprotein E-derived arginine-rich peptides improves their cell penetration capability.Scientific reports · 2023Article
- Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides.International journal of molecular sciences · 2022Review
- Alternative Antibiotics in Dentistry: Antimicrobial Peptides.Pharmaceutics · 2022Review
- How lipids affect the energetics of co-translational alpha helical membrane protein folding.Biochemical Society transactions · 2022Review
- Cotranslational recruitment of ribosomes in protocells recreates a translocon-independent mechanism of proteorhodopsin biogenesis.iScience · 2021Article
- Naphthalimide-Containing BP100 Leads to Higher Model Membranes Interactions and Antimicrobial Activity.Biomolecules · 2021Article
- Expanding MPEx Hydropathy Analysis to Account for Electrostatic Contributions to Protein Interactions with Anionic Membranes.The Journal of membrane biology · 2021Article
- Electrostatic effects in saturation of membrane binding of cationic cell-penetrating peptide.European biophysics journal : EBJ · 2021Article
- In Silico Prediction of the Binding, Folding, Insertion, and Overall Stability of Membrane-Active Peptides.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Backbone Hydrogen Bond Energies in Membrane Proteins Are Insensitive to Large Changes in Local Water Concentration.Journal of the American Chemical Society · 2020Article
- Ions Modulate Key Interactions between pHLIP and Lipid Membranes.Biophysical journal · 2019Article
- The importance of the membrane interface as the reference state for membrane protein stability.Biochimica et biophysica acta. Biomembranes · 2018Article
- Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.Probiotics and antimicrobial proteins · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The free energy cost ΔG of partitioning many unfolded peptides into membrane interfaces is unfavorable due to the cost of partitioning backbone peptide bonds. The partitioning cost is dramatically reduced if the peptide bonds participate in hydrogen bonds. The reduced cost underlies secondary structure formation by amphiphilic peptides partitioned into membrane interfaces through a process referred to as partitioning-folding coupling. This coupling is characterized by the free energy reduction per residue, ∆G(res) that drives folding. There is some debate about the correct value of ∆G(res) and its dependence on the hydrophobic moment (μ(H)) of amphiphilic α-helical peptides. We show how to compute ∆G(res) correctly. Using published data for two families of peptides with different hydrophobic moments and charges, we find that ∆G(res) does not depend upon μ(H). The best estimate of ∆G(res) is -0.37 ± 0.02 kcal mol(-1). This article is part of a Special Issue entitled: Membrane protein structure and function.
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Registered trials
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