High-Speed Atomic Force Microscopy to Study Myosin Motility

被引：2
|
作者：
Kodera, Noriyuki [1 ]
Ando, Toshio [1 ]
机构：
[1] Kanazawa Univ, Nano Life Sci Inst WPI NanoLSI, Kanazawa, Ishikawa, Japan
来源：
MYOSINS: A SUPERFAMILY OF MOLECULAR MOTORS, 2ND EDITION | 2020年 / 1239卷
关键词：
High-speed atomic force microscopy; Myosin ATPase; Molecular motor; Chemo-mechanical coupling; Single-molecule measurement; HAND-OVER-HAND; SINGLE-MOLECULE; PROCESSIVE MYOSIN; ACTOMYOSIN-V; MOTOR DOMAIN; BIOMOLECULAR PROCESSES; STRUCTURAL DYNAMICS; STEPPING KINETICS; POWER STROKE; COILED-COIL;
D O I：
10.1007/978-3-030-38062-5_7
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
High-speed atomic force microscopy (HS-AFM) is a unique tool that enables imaging of protein molecules during their functional activity at sub-100 ms temporal and submolecular spatial resolution. HS-AFM is suited for the study of highly dynamic proteins, including myosin motors. HS-AFM images of myosin V walking on actin filaments provide irrefutable evidence for the swinging lever arm motion propelling the molecule forward. Moreover, molecular behaviors that have not been noticed before are also displayed on the AFM movies. This chapter describes the principle, underlying techniques and performance of HS-AFM, filmed images of myosin V, and mechanistic insights into myosin motility provided from the filmed images.
引用
收藏
页码：127 / 152
页数：26
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