STRUCTURE AT 2.5 ANGSTROM OF A DESIGNED PEPTIDE THAT MAINTAINS SOLUBILITY OF MEMBRANE-PROTEINS

被引：162

作者：

SCHAFMEISTER, CE

MIERCKE, LJW

STROUD, RM

机构：

[1] Department of Biochemistry and Biophysics, University of California, San Francisco

来源：

SCIENCE | 1993年 / 262卷 / 5134期

关键词：

D O I：

10.1126/science.8235592

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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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页码：734 / 738

页数：5

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