Greenberg Michael J, Shuman Henry, Ostap E Michael
Department of Physiology, The Pennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Ave., Campus Box 8231, St. Louis, MO, 63110, USA.
Methods Mol Biol. 2017;1486:483-509. doi: 10.1007/978-1-4939-6421-5_19.
The myosin superfamily of molecular motors utilizes energy from ATP hydrolysis to generate force and motility along actin filaments in a diverse array of cellular processes. These motors are structurally, kinetically, and mechanically tuned to their specific molecular roles in the cell. Optical trapping techniques have played a central role in elucidating the mechanisms by which myosins generate force and in exposing the remarkable diversity of myosin functions. Here, we present thorough methods for measuring and analyzing interactions between actin and non-processive myosins using optical trapping techniques.
分子马达的肌球蛋白超家族利用ATP水解产生的能量，在各种细胞过程中沿着肌动蛋白丝产生力和运动。这些马达在结构、动力学和机械方面都根据其在细胞中的特定分子作用进行了调整。光镊技术在阐明肌球蛋白产生力的机制以及揭示肌球蛋白功能的显著多样性方面发挥了核心作用。在这里，我们介绍了使用光镊技术测量和分析肌动蛋白与非连续性肌球蛋白之间相互作用的详细方法。
