ArticleProceedings of the National Academy of Sciences of the United States of America2011
Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 205 papers.
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Who cites it
205 citing papers in PubMed, 333 citations in OpenAlex.
- A unified framework for potency-oriented AMP discovery via multi-modal learning and guided sequence synthesis.PLoS computational biology · 2026Article
- Lipid-Shell PARCH: A Physically Motivated Scale for Transmembrane Residue Hydropathy.The journal of physical chemistry. B · 2026Article
- Membrane-Traversing Peptides: Mechanistic Landscapes, Assays, and Applications.Chemical reviews · 2026Review
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
- Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin.The Journal of biological chemistry · 2026Article
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin.bioRxiv : the preprint server for biology · 2026Article
- Implicit membrane for helical peptide selectivity toward bacterial membranes.Biophysical journal · 2026Article
- Trp-containing Peptides with Therapeutic Potential for Cutibacterium acnes Infection.Probiotics and antimicrobial proteins · 2026Article
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Membrane insertion and dimerization of glycophorin-A mutations studied by free energy simulations.Biophysical journal · 2026Article
- The Blobulator: A Toolkit for Identification and Visual Exploration of Hydrophobic Modularity in Protein Sequences.Journal of chemical information and modeling · 2026Article
- Rational tuning of temperature sensitivity of the TRPM8 channel.EMBO reports · 2025Article
- Packing of apolar amino acids is not a strong stabilizing force in transmembrane helix dimerization.Biophysical journal · 2025Article
- The blobulator: a toolkit for identification and visual exploration of hydrophobic modularity in protein sequences.bioRxiv : the preprint server for biology · 2025Article
- Structural diversity and evolutionary constraints of oxidative phosphorylation.Cell genomics · 2025Article
- Structure-Antimicrobial Activity Relationships of Recombinant Host Defence Peptides Against Drug-Resistant Bacteria.Microbial biotechnology · 2025Article
- Structure, assembly and inhibition of the Toxoplasma gondii respiratory chain supercomplex.Nature structural & molecular biology · 2025Article
- The lipid bilayer strengthens the cooperative network of membrane proteins.Science advances · 2025Article
145 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The transfer free energies of the twenty natural amino acid side chains from water to phospholipid bilayers make a major contribution to the assembly and function of membrane proteins. Measurements of those transfer free energies will facilitate the identification of membrane protein sequences and aid in the understanding of how proteins interact with membranes during key biological events. We report the first water-to-bilayer transfer free energy scale (i.e., a "hydrophobicity scale") for the twenty natural amino acid side chains measured in the context of a native transmembrane protein and a phospholipid bilayer. Our measurements reveal parity for apolar side-chain contributions between soluble and membrane proteins and further demonstrate that an arginine side-chain placed near the middle of a lipid bilayer is accommodated with much less energetic cost than predicted by molecular dynamics simulations.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.