The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
Open accessAbstract
▪ Abstract Stably folded membrane proteins reside in a free energy minimum determined by the interactions of the peptide chains with each other, the lipid bilayer hydrocarbon core, the bilayer interface, and with water. The prediction of three-dimensional structure from sequence requires a detailed understanding of these interactions. Progress toward this objective is summarized in this review by means of a thermodynamic framework for describing membrane protein folding and stability. The framework includes a coherent thermodynamic formalism for determining and describing the energetics of peptide-bilayer interactions and a review of the properties of the environment of membrane proteins—the bilayer milieu. Using a four-step thermodynamic cycle as a guide, advances in three main aspects of membrane protein folding energetics are discussed: protein binding and folding in bilayer interfaces, transmembrane helix insertion, and helix-helix interactions. The concepts of membrane protein stability that emerge provide insights to fundamental issues of protein folding.
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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253
Siderophore-Mediated Iron Transport: Crystal Structure of FhuA with Bound Lipopolysaccharide
Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., & Welte, W. (1998) · Science · doi:10.1126/science.282.5397.2215 · Cited by 787
Cited by
Lipid–protein interactions in biological membranes: A structural perspective
Lee, A. G. (2003) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(03)00056-7 · Cited by 886
Plasma membrane phosphoinositide organization by protein electrostatics
McLaughlin, S., & Murray, D. (2005) · Nature · doi:10.1038/nature04398 · Cited by 868
von Heijne, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2063 · Cited by 538
Ballesteros, J. A., Shi, L., & Javitch, J. A. (2001) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)08985-5 · Cited by 438
Conserved and Cooperative Assembly of Membrane-Bound α-Helical States of Islet Amyloid Polypeptide
Knight, J. D., Hebda, J. A., & Miranker, A. D. (2006) · Biochemistry · doi:10.1021/bi060579z · Cited by 309
Metadata
- Authors
- White, S. H., & Wimley, W. C.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 1999-06
- Volume
- 28
- Issue
- 1
- Pages
- 319-365
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2155147384
- Cited by
- 1,764
- References
- 3
- FWCI
- 20.66
- Type
- journal article
- Language
- en
- Open access
- green
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- White, S. H., & Wimley, W. C. (1999). MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.28.1.319
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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