Force as a single molecule probe of multidimensional protein energy landscapes.
Force as a single molecule probe of multidimensional protein energy landscapes.
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DOI：
10.1016/j.sbi.2012.11.007
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发表时间：
2013-02
影响因子：
6.8
通讯作者：
G. Žoldák;M. Rief
中科院分区：
文献类型：
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作者：
G. Žoldák;M. Rief
力谱学已经发展成为实时研究蛋白质在单分子水平上折叠和结合的不可或缺的工具。拉力几何结构的设计允许以非常精确的方式调整反应坐标。最近的许多实验都利用了这种可能性，并提供了对复杂高维能量景观上的折叠路径的详细洞察。除了提供对反应坐标的控制之外，力也是一个重要的生理参数，在体内条件下影响蛋白质的构象。单分子力谱研究已经开始解开受力蛋白质结构对机械负荷的响应和适应。
Force spectroscopy has developed into an indispensable tool for studying folding and binding of proteins on a single molecule level in real time. Design of the pulling geometry allows tuning the reaction coordinate in a very precise manner. Many recent experiments have taken advantage of this possibility and have provided detailed insight the folding pathways on the complex high dimensional energy landscape. Beyond its potential to provide control over the reaction coordinate, force is also an important physiological parameter that affects protein conformation under in vivo conditions. Single molecule force spectroscopy studies have started to unravel the response and adaptation of force bearing protein structures to mechanical loads.