MEMPHYS-Center for Biomembrane Physics, Institute of Physics and Chemistry, University of Southern Denmark, Odense, Denmark.
MEMPHYS-Center for Biomembrane Physics, Institute of Physics and Chemistry, University of Southern Denmark, Odense, Denmark; Department of Physics, Jagiellonian University, Cracow, Poland; Institute of Complex Systems 7: Biomechanics, Forschungszentrum Jülich, Jülich, Germany.
Biophys J. 2013 Dec 17;105(12):2771-80. doi: 10.1016/j.bpj.2013.10.030.
Dynamic force spectroscopy was used to test force-induced dissociation of the complex between the integrin α7β1 and the bacterial protein invasin. Both proteins were used in truncated forms comprising the respective binding sites. Using the biomembrane force-probe, the bond system was exposed to 14 different loading rates ranging from 18 pN/s to 5.3 nN/s. At each rate, bond rupture spectra were collected. Median forces ranged from 8 to 72 pN. These showed two linear regimes when plotted against the logarithm of the force-loading rate. However, a statistical analysis of the full rupture force spectra including the detection limits of the setup showed that all measured data are well described by dissociation over a single barrier.
动态力谱技术被用于测试整合素 α7β1 与细菌蛋白入侵素复合物在受力时的解离情况。这两种蛋白质都以包含各自结合位点的截断形式使用。使用生物膜力探针，将键系统暴露于 14 种不同的加载速率下，范围从 18 pN/s 到 5.3 nN/s。在每种速率下，都收集了键断裂光谱。中值力范围为 8 到 72 pN。当这些力值与力加载速率的对数作图时，呈现出两个线性区域。然而，对包括设置检测限在内的完整断裂力谱的统计分析表明，所有测量数据都很好地通过单个势垒的解离来描述。
