Chemomechanical coupling in actomyosin system: An approach by in vitro movement assay and kinetic analysis of ATP hydrolysis by shortening myofibrils |
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| Affiliation: | 1. Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Toyonaka, Osaka 560, Japan;7. Department of Biochemistry, Okayama University Dental School, Okayama 700, Japan;1. School of Pharmaceutical Sciences, Tsinghua-Peking Joint Center for Life Sciences, IDG/McGovern Institute for Brain Research, Tsinghua University, Beijing, 100084, China;1. State Key Laboratory of Medical Neurobiology and MOE Frontiers Center for Brain Science, Department of Neurosurgery at Huashan Hospital, Human Phenome Institute, Ministry of Education Key Laboratory of Contemporary Anthropology, Collaborative Innovation Center of Genetics and Development, Institute of Brain Science, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, 2005 Songhu Road, Yangpu District, Shanghai 200438, China;2. State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Multiscale Research Institute for Complex Systems, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, Shanghai 200438, China;3. Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan;1. Departments of Otolaryngology and Neurology, Boston Children’s Hospital and Harvard Medical School, Boston, MA 02115, USA;2. Department of Neurobiology and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA;3. Molecular Biology and Genetics Section, National Institute on Deafness and Other Communication Disorders, NIH, Bethesda, MD 20892, USA;4. Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA;1. Key Laboratory for Micro/Nano Optoelectronic Devices of Ministry of Education & Hunan Provincial Key Laboratory of Low-Dimensional Structural Physics and Devices, School of Physics and Electronics, Hunan University, Changsha 410082, China;2. Ningbo Institute of Materials Technology and Engineering, Chinese Academy of Sciences, Ningbo 315201, China;3. Shenzhen Lubon Technology Co. Ltd, Shenzhen 518000, China |
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| Abstract: | On the basis of our recent studies of the sliding distance of actin filaments during one ATP cycle on the surface of myosin-coated glass surface and ATP hydrolysis by rapidly shortening myofibrils, the molecular mechanism of chemomechanical coupling is considered. We conclude that the myosin head can repeat many active cyclic interactions with actins to drive the actin filaments over a long distance during one ATP cycle, and that the distance is variable depending on the load. |
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