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Hydrophobic organization of membrane proteins

Rees, D. C. and DeAntonio, L. and Eisenberg, D. (1989) Hydrophobic organization of membrane proteins. Science, 245 (4917). pp. 510-513. ISSN 0036-8075. doi:10.1126/science.2667138.

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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.

Item Type:Article
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URLURL TypeDescription DOIArticle
Rees, D. C.0000-0003-4073-1185
Additional Information:© 1989 American Association for the Advancement of Science. 3 March 1989, accepted 2 June 1989. We thank J. P. Allen and G. Feher for helpful discussions. Supported by NIH grants GM31299 and GM39558. D.G.R. is an A. P. Sloan research fellow. Programs and sequence alignments used in this work are available from D.G.R.
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Alfred P. Sloan FoundationUNSPECIFIED
Issue or Number:4917
Record Number:CaltechAUTHORS:20150204-145844789
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Official Citation:Rees, D., DeAntonio, L., & Eisenberg, D. (1989). Hydrophobic organization of membrane proteins. Science, 245(4917), 510-513. doi: 10.1126/science.2667138
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:54387
Deposited On:05 Feb 2015 04:52
Last Modified:10 Nov 2021 20:32

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