The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Hydrophobic Organization of Membrane Proteins
Abstract
Membrane-exposed residues are more hydrophobic than buried interior residues in the transmembrane regions of the photosynthetic reaction center from Rhodobacter sphaeroides . This hydrophobic organization is opposite to that of water-soluble proteins. The relative polarities of interior and surface residues of membrane and water soluble proteins are not simply reversed, however. The hydrophobicities of interior residues of both membrane and water-soluble proteins are comparable, whereas the bilayer-exposed residues of membrane proteins are more hydrophobic than the interior residues, and the aqueous-exposed residues of water-soluble proteins are more hydrophilic than the interior residues. A method of sequence analysis is described, based on the periodicity of residue replacement in homologous sequences, that extends conclusions derived from the known atomic structure of the reaction center to the more extensive database of putative transmembrane helical sequences.
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Cites
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Self-citationMolecular Genetics of Human Color Vision: The Genes Encoding Blue, Green, and Red Pigments
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MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
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Metadata
- Authors
- Rees, D. C., DeAntonio, L., & Eisenberg, D.
- Venue
- Science
- Published
- 1989-08-04
- Volume
- 245
- Issue
- 4917
- Pages
- 510-513
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1994340275
- Cited by
- 311
- References
- 48
- FWCI
- 6.32
- Type
- journal article
- Language
- en
- Open access
- closed
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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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