Chemical Physics Letters ( IF 2.8 ) Pub Date : 2017-11-20 , DOI: 10.1016/j.cplett.2017.11.025 Tatsuya Yamada , Shigeki Mitaku , Takahisa Yamato
Single-molecule force spectroscopy by atomic force microscopy allows us to get insight into the mechanical unfolding of membrane proteins, and a typical experiment exhibits characteristic patterns on the force distance curves. The origin of these patterns, however, has not been fully understood yet. We performed coarse-grained simulation of the forced unfolding of halorodopsin, reproduced the characteristic features of the experimental force distance curves. A further examination near the membrane-water interface indicated the existence of a motif for the force peak formation, i.e., the occurrence of hydrophobic residues in the upper interface region and hydrophilic residues below the lower interface region.
中文翻译:
膜蛋白机械展开中间体的粗粒分子动力学模拟表征
通过原子力显微镜的单分子力光谱学,我们可以洞悉膜蛋白的机械展开,并且典型的实验在力距曲线上表现出特征性模式。但是,这些模式的起源还没有被完全理解。我们进行了卤代鱼青素强制展开的粗粒模拟,再现了实验力距离曲线的特征。在膜-水界面附近的进一步检查表明存在用于力峰形成的基序,即,在上部界面区域中存在疏水性残基,而在下部界面区域下方存在亲水性残基。