Single molecule measurements of titin elasticity.
Single molecule measurements of titin elasticity.
复制标题
肌动蛋白弹性的单分子测量。
DOI：
10.1016/s0079-6107(01)00009-8
复制
发表时间：
2001
影响因子：
3.8
通讯作者：
Jin,AJ
中科院分区：
文献类型：
--
作者：
Wang,K;Forbes,JG;Jin,AJ
Titin具有巨大的3-4MDa单链和多个模块基序，横跨骨骼肌和心肌的半肌节，具有重要的多方面功能。近年来，Titin已成为原子力显微镜(AFM)和激光光阱(LOT)观察单分子的热门对象。在这里，我们回顾了这些单Titin分子延伸研究，重点是了解它们与肌肉功能中的Titin弹性的相关性。介绍了研究Titin单分子的一些基本方法，包括动态力的应用、丝状Titin模体的弹性模型、AFM和Lot的技术基础和校准以及Titin样品的制备。按时间顺序回顾了最近关于单项延展观测的主要出版物。随后是对Titin结构域折叠/展开结果和丝状Titin基序的弹性性质的总结评估。讨论了这些单项Titin测量对肌肉生理学/病理学的影响，并对单项Titin研究的未来进展进行了展望。
Titin, with a massive single chain of 3–4MDa and multiple modular motifs, spans the half-sarcomere of skeletal and cardiac muscles and serves important, multifaceted functions. In recent years, titin has become a favored subject of single molecule observations by atomic force microscopy (AFM) and laser optical trap (LOT). Here we review these single titin molecule extension studies with an emphasis on understanding their relevance to titin elasticity in muscle function. Some fundamental aspects of the methods for single titin molecule investigations, including the application of dynamic force, the elasticity models for filamentous titin motifs, the technical foundations and calibrations of AFM and LOT, and titin sample preparations are provided. A chronological review of major publications on recent single titin extension observations is presented. This is followed by summary evaluations of titin domain folding/unfolding results and of elastic properties of filamentous titin motifs. Implications of these single titin measurements for muscle physiology/pathology are discussed and forthcoming advances in single titin studies are anticipated.