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骨骼肌肌球蛋白II的结构与功能。

Skeletal muscle myosin II structure and function.

作者信息

Lutz G J, Lieber R L

机构信息

Department of Orthopaedics, University of California at San Diego School of Medicine, USA.

出版信息

Exerc Sport Sci Rev. 1999;27:63-77.

Abstract

Recent experimental advances in structural biology, biophysics, and molecular biology have dramatically increased our understanding of the molecular mechanism of muscle contraction, as well as the assembly of myosin filaments. Future studies are required to detail, for example, the molecular cause of the conformational change during the power stroke and ATP hydrolysis, as well as the nature of the communication between nucleotide and actin binding sites. Based on the structural and functional homology between myosin and other molecular motors, these findings have implications not only for understanding muscle contraction, but for understanding numerous aspects of motility in all cellular systems as well.

摘要

结构生物学、生物物理学和分子生物学领域最近的实验进展极大地增进了我们对肌肉收缩分子机制以及肌球蛋白丝组装的理解。例如,未来的研究需要详细阐明动力冲程和ATP水解过程中构象变化的分子原因,以及核苷酸与肌动蛋白结合位点之间通讯的本质。基于肌球蛋白与其他分子马达之间的结构和功能同源性,这些发现不仅对理解肌肉收缩有意义,对理解所有细胞系统中运动的诸多方面也有意义。

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