A successful change of circumstance: a transition state for membrane protein folding
A successful change of circumstance: a transition state for membrane protein folding
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DOI：
10.1016/j.sbi.2012.03.008
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发表时间：
2012-08-01
影响因子：
6.8
通讯作者：
Booth, Paula J.
中科院分区：
文献类型：
--
作者：
Booth, Paula J.
了解过渡态是理解反应机制的关键。对于完整的膜蛋白折叠来说，这一重要信息一直缺乏，但现在最新的进展让人们深入了解了其折叠过渡状态的结构。这一进展是通过将经典蛋白质工程方法（phi 值分析）从水溶性蛋白质成功转化为疏水性膜嵌入蛋白质类别而取得的。本综述涵盖了 α 螺旋膜蛋白折叠的过渡态。过渡状态下的螺旋形成与序列位置和跨膜插入细胞膜的顺序相关，表明在与天然膜完全不同的条件下的体外测量可以反映细胞情况。
Knowledge of the transition state is key to understanding a reaction mechanism. This vital information has been lacking for integral membrane protein folding, but now recent advances have given insight into the structure of their folding transition state. This progress has arisen through the successful translation of a classical protein engineering method, phi value analysis, from water-soluble proteins to the hydrophobic, membrane-embedded protein class. This review covers the transition state for the folding of alpha helical membrane proteins. Helix formation in the transition state correlates with sequence position and the order of transmembrane insertion into the cell membrane, showing that in vitro measurements, in entirely different conditions to natural membranes, may reflect the cellular situation.