当前位置: X-MOL 学术Annu. Rev. Anal. Chem. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Single-Molecule Force Spectroscopy of Transmembrane β-Barrel Proteins
Annual Review of Analytical Chemistry ( IF 8 ) Pub Date : 2018-06-12 00:00:00 , DOI: 10.1146/annurev-anchem-061417-010055
Johannes Thoma 1 , K. Tanuj Sapra , Daniel J. Müller 1
Affiliation  

Single-molecule force spectroscopy (SMFS) has been widely applied to study the mechanical unfolding and folding of transmembrane proteins. Here, we review the recent progress in characterizing bacterial and human transmembrane β-barrel proteins by SMFS. First, we describe the mechanical unfolding of transmembrane β-barrels, which follows a general mechanism dictated by the sequential unfolding and extraction of individual β-strands and β-hairpins from membranes. Upon force relaxation, the unfolded polypeptide can insert stepwise into the membrane as single β-strands or β-hairpins to fold as the native β-barrel. The refolding can be followed at a high spatial and temporal resolution, showing that small β-barrels are able to fold without assistance, whereas large and complex β-barrels require chaperone cofactors. Applied in the dynamic mode, SMFS can quantify the kinetic and mechanical properties of single β-hairpins and reveal complementary insight into the membrane protein structure and function relationship. We further outline the challenges that SMFS experiments must overcome for a comprehensive understanding of the folding and function of transmembrane β-barrel proteins.

中文翻译:


跨膜β-桶蛋白的单分子力谱

单分子力谱(SMFS)已被广泛用于研究跨膜蛋白的机械展开和折叠。在这里,我们回顾了通过SMFS表征细菌和人跨膜β-桶蛋白的最新进展。首先,我们描述跨膜β桶的机械展开,该过程遵循一般机制,该机制由依次展开和从膜中提取单个β链和β发夹结构决定。力松弛后,未折叠的多肽可以逐步以单个β链或β发夹的形式插入膜中,以折叠为天然β桶。可以在高空间和时间分辨率下进行重新折叠,这表明小β桶无需辅助即可折叠,而大而复杂的β桶则需要分子伴侣辅助因子。在动态模式下应用 SMFS可以量化单个β-发夹的动力学和机械性质,并揭示对膜蛋白结构和功能关系的补充见解。我们进一步概述了SMFS实验必须克服的挑战,以全面了解跨膜β-桶蛋白的折叠和功能。

更新日期:2018-06-12
down
wechat
bug