Reports

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

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Science  29 Oct 1993:
Vol. 262, Issue 5134, pp. 734-738
DOI: 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.

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