Structure at 2.5 Å of a Designed Peptide that Maintains Solubility of Membrane Proteins
- 29 October 1993
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 262 (5134) , 734-738
- https://doi.org/10.1126/science.8235592
Abstract
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.Keywords
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