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Science 29 October 1993:
Vol. 262. no. 5134, pp. 734 - 738
DOI: 10.1126/science.8235592
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Articles

Science, Vol 262, Issue 5134, 734-738
Copyright © 1993 by American Association for the Advancement of Science

articles

Structure at 2.5 A of a designed peptide that maintains solubility of membrane proteins

CE Schafmeister, LJ Miercke, and RM Stroud

Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.

A 24-amino acid peptide designed to solubilize integral membrane proteins has been synthesized. The design was for an amphipathic alpha helix with a "flat" hydrophobic surface that would interact with a transmembrane protein as a detergent. When mixed with peptide, 85 percent of bacteriorhodopsin and 60 percent of rhodopsin remained in solution over a period of 2 days in their native forms. The crystal structure of peptide alone showed it to form an antiparallel four-helix bundle in which monomers interact, flat surface to flat surface, as predicted.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Designer short peptide surfactants stabilize G protein-coupled receptor bovine rhodopsin.
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De novo design of an IL-4 antagonist and its structure at 1.9 A.
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Engineering of a Water-Soluble Plant Cytochrome P450, CYP73A1, and NMR-Based Orientation of Natural and Alternate Substrates in the Active Site.
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Amphiphilic biopolymers (amphibiopols) as new surfactants for membrane protein solubilization.
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Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions.
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   Abstract »    Full Text »    PDF »
Protein Design: A Hierarchic Approach.
J. W. Bryson, S. F. Betz, H. S. Lu, D. J. Suich, H. X. Zhou, K. T. O'Neil, and W. F. DeGrado (1995)
Science 270, 935-941
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Science. ISSN 0036-8075 (print), 1095-9203 (online)