STRUCTURE AT 2.5 ANGSTROM OF A DESIGNED PEPTIDE THAT MAINTAINS SOLUBILITY OF MEMBRANE-PROTEINS
STRUCTURE AT 2.5 ANGSTROM OF A DESIGNED PEPTIDE THAT MAINTAINS SOLUBILITY OF MEMBRANE-PROTEINS
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DOI：
10.1126/science.8235592
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发表时间：
1993-10-29
期刊：
影响因子：
56.9
通讯作者：
STROUD, RM
中科院分区：
文献类型：
--
作者：
SCHAFMEISTER, CE;MIERCKE, LJW;STROUD, RM
合成了一种可溶解完整膜蛋白的24个氨基酸的多肽。这项设计是为了设计一种两亲性的阿尔法螺旋，它的疏水表面“平坦”，可以作为洗涤剂与跨膜蛋白相互作用。当与多肽混合时，85%的细菌视紫红质和60%的视紫红质以其天然形式保持在溶液中超过2天。单是多肽的晶体结构就表明，它形成了一个反平行的四螺旋链束，单体在其中相互作用，平面到平面，正如预测的那样。
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.