Ahn K, Chen D, Kemper B
Department of Physiology and Biophysics, University of Illinois at Urbana-Champaign 61801.
Biochim Biophys Acta. 1994 Dec 30;1224(3):459-62. doi: 10.1016/0167-4889(94)90283-6.
To investigate the dependence of transmembrane translocation on the hydrophobic moment of the hydrophobic core of the preproparathyroid hormone signal sequence, amino acids were switched to maximize or minimize the hydrophobic moment without changing the length or overall hydrophobicity of the core. As assayed in an in vitro translation system with microsomal membranes, the efficiency of translocation of these mutants was inversely related to the hydrophobic moment, indicating the hydrophobic moment or a related property may contribute to translocational activity.
为了研究甲状旁腺激素原信号序列疏水核心的疏水矩对跨膜转运的依赖性,对氨基酸进行了置换,以在不改变核心长度或整体疏水性的情况下最大化或最小化疏水矩。在含有微粒体膜的体外翻译系统中进行测定时,这些突变体的转运效率与疏水矩呈负相关,这表明疏水矩或一种相关特性可能有助于转运活性。