The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
Open accessAbstract
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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Antimicrobial Peptides: An Update on Classifications and Databases
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Documentation of an Imperative To Improve Methods for Predicting Membrane Protein Stability
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Interpreting the molecular mechanisms of disease variants in human transmembrane proteins
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Metadata
- Authors
- Moon, C. P., & Fleming, K. G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2011-05-23
- Volume
- 108
- Issue
- 25
- Pages
- 10174-10177
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2019215286
- Cited by
- 332
- References
- 31
- FWCI
- 9.87
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
