Stepwise unfolding of titin under force-clamp atomic force microscopy.
Stepwise unfolding of titin under force-clamp atomic force microscopy.
复制标题
DOI：
10.1073/pnas.98.2.468
复制
发表时间：
2001-01
影响因子：
11.1
通讯作者：
A. Oberhauser;P. Hansma;M. Carrión-Vázquez;Julio M. Fernandez
中科院分区：
文献类型：
--
作者：
A. Oberhauser;P. Hansma;M. Carrión-Vázquez;Julio M. Fernandez
在这里，我们演示了适用于原子力显微镜的单分子力夹的实现。我们证明了在力钳条件下，工程化的Titin蛋白由于其模块的展开而逐步伸长，并且等待展开的时间呈指数分布。力钳测量直接测量展开概率的力依赖关系，并容易捕捉到人类心脏肌动蛋白I27和I28模块的不同机械稳定性。力钳光谱学有望成为探索弹性蛋白质机械稳定性的直接方法，例如在肌肉、细胞外基质和细胞黏附中发现的那些蛋白质。
Here we demonstrate the implementation of a single-molecule force clamp adapted for use with an atomic force microscope. We show that under force-clamp conditions, an engineered titin protein elongates in steps because of the unfolding of its modules and that the waiting times to unfold are exponentially distributed. Force-clamp measurements directly measure the force dependence of the unfolding probability and readily captures the different mechanical stability of the I27 and I28 modules of human cardiac titin. Force-clamp spectroscopy promises to be a direct way to probe the mechanical stability of elastic proteins such as those found in muscle, the extracellular matrix, and cell adhesion.