微管相关运动中驱动蛋白的动力学图和自由能图。

Kinetic diagram and free energy diagram for kinesin in microtubule-related motility.

作者信息

Hill T L

出版信息

Proc Natl Acad Sci U S A. 1986 May;83(10):3326-30. doi: 10.1073/pnas.83.10.3326.

DOI:10.1073/pnas.83.10.3326

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC323506/

Abstract

The theoretical formalism that shows how biochemistry (ATPase activity) is related to mechanics in muscle contraction can be extended to the role of kinesin in microtubule-related motility. The main features added are the freedom of kinesin molecules to come and go from the motility complex and the small number of operative kinesin molecules in some systems. The starting points for this kind of approach are the kinetic diagram of biochemical states and the corresponding free energy diagram for these states. These topics are introduced and discussed here in relation to those systems that are presumed to use kinesin.

摘要

展示生物化学（ATP酶活性）如何与肌肉收缩中的力学相关的理论形式体系，可扩展到驱动蛋白在微管相关运动中的作用。增加的主要特征是驱动蛋白分子进出运动复合体的自由度以及某些系统中起作用的驱动蛋白分子数量较少。这种方法的出发点是生化状态的动力学图以及这些状态相应的自由能图。本文结合那些假定使用驱动蛋白的系统来介绍和讨论这些主题。

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引用本文的文献

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2

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