Leibniz Institute of Molecular Pharmacology (FMP), Robert-Rössle-Str. 10, 13125, Berlin, Germany.
Cell Mol Life Sci. 2010 Jun;67(11):1779-98. doi: 10.1007/s00018-010-0259-0. Epub 2010 Jan 27.
Separation of cells and organelles by bilayer membranes is a fundamental principle of life. Cellular membranes contain a baffling variety of proteins, which fulfil vital functions as receptors and signal transducers, channels and transporters, motors and anchors. The vast majority of membrane-bound proteins contain bundles of alpha-helical transmembrane domains. Understanding how these proteins adopt their native, biologically active structures in the complex milieu of a membrane is therefore a major challenge in today's life sciences. Here, we review recent progress in the folding, unfolding and refolding of alpha-helical membrane proteins and compare the molecular interactions that stabilise proteins in lipid bilayers. We also provide a critical discussion of a detergent denaturation assay that is increasingly used to determine membrane-protein stability but is not devoid of conceptual difficulties.
双层膜将细胞和细胞器分隔开是生命的基本原理。细胞膜含有各种各样的蛋白质，这些蛋白质作为受体和信号转导物、通道和转运蛋白、马达和锚定物，发挥着至关重要的作用。绝大多数膜结合蛋白含有束状的α-螺旋跨膜结构域。因此，了解这些蛋白质如何在膜的复杂环境中形成其天然的、具有生物活性的结构，是当今生命科学的主要挑战之一。在这里，我们回顾了α-螺旋膜蛋白折叠、展开和重折叠的最新进展，并比较了稳定脂质双层中蛋白质的分子相互作用。我们还对去污剂变性测定法进行了批判性讨论，这种方法越来越多地用于测定膜蛋白的稳定性，但它并非没有概念上的困难。
