Retinal proteins as model systems for membrane protein folding.
Retinal proteins as model systems for membrane protein folding.
复制标题
视网膜蛋白作为膜蛋白折叠的模型系统。
DOI：
10.1016/j.bbabio.2013.11.021
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
Tastan O
中科院分区：
文献类型：
--
作者：
Tastan O
膜蛋白的实验性折叠研究比水溶性蛋白更具挑战性，因为膜嵌入序列的疏水性含量更高，并且需要为跨膜区域提供疏水环境。第一个挑战是它们的变性：由于膜中极性基团的热力学不稳定性，膜蛋白的二级结构比可溶性蛋白更难破坏。第二个挑战是从变性状态重新折叠。膜蛋白的成功重折叠几乎总是从非常微妙的变性状态开始。因此，使用计算方法分析膜蛋白折叠是有用的，我们将提供使用Floppy Inclusions and Rigid Substructure Topography（FIRST）方法模拟膜蛋白结构展开的结果。计算方法的优势在于它们允许在不同的膜蛋白之间进行直接比较。在这里，我们将审查，实验和第一研究的视网膜结合蛋白bacteriorhodopsin和哺乳动物视紫红质，并讨论扩展的研究结果，推导出的膜蛋白折叠的机制的假设一般。这篇文章是特刊的一部分，题目是：视网膜蛋白质-你可以教老狗新把戏。
Experimental folding studies of membrane proteins are more challenging than water-soluble proteins because of the higher hydrophobicity content of membrane embedded sequences and the need to provide a hydrophobic milieu for the transmembrane regions. The first challenge is their denaturation: due to the thermodynamic instability of polar groups in the membrane, secondary structures in membrane proteins are more difficult to disrupt than in soluble proteins. The second challenge is to refold from the denatured states. Successful refolding of membrane proteins has almost always been from very subtly denatured states. Therefore, it can be useful to analyze membrane protein folding using computational methods, and we will provide results obtained with simulated unfolding of membrane protein structures using the Floppy Inclusions and Rigid Substructure Topography (FIRST) method. Computational methods have the advantage that they allow a direct comparison between diverse membrane proteins. We will review here both, experimental and FIRST studies of the retinal binding proteins bacteriorhodopsin and mammalian rhodopsin, and discuss the extension of the findings to deriving hypotheses on the mechanisms of folding of membrane proteins in general. This article is part of a Special Issue entitled: Retinal Proteins—You can teach an old dog new tricks.
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