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相关论文: Elastic lever arm model for myosin V

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The assumption of linear response of protein molecules to thermal noise or structural perturbations, such as ligand binding or detachment, is broadly used in the studies of protein dynamics. Conformational motions in proteins are…

生物大分子 · 定量生物学 2010-06-21 Yuichi Togashi , Toshio Yanagida , Alexander S. Mikhailov

We have proposed the neck linker swing model to investigate the mechanism of mechanochemical coupling of kinesin. The Michaelis-Menten-like curve for velocity vs ATP concentration at different loads has been obtained, which is in agreement…

其他定量生物学 · 定量生物学 2007-05-23 Yaogen Shu , Hualin Shi

Mechanically induced folding of passive cross-linkers is a fundamental biological phenomenon. A typical example is a conformational change in myosin II responsible for the power-stroke in skeletal muscles. In this paper we present an…

生物物理 · 物理学 2017-09-14 Matthieu Caruel , Jean-Marc Allain , Lev Truskinovsky

Cellular cargo can be bound to cytoskeletal filaments by one or multiple active or passive molecular motors. Recent experiments have shown that the presence of auxiliary, nondriving motors, results in an enhanced processivity of the cargo,…

生物大分子 · 定量生物学 2019-03-27 Filippo Posta , Maria R. D'Orsogna , Tom Chou

Conventional kinesin is a two-headed homodimeric motor protein, which is able to walk along microtubules processively by hydrolyzing ATP. Its neck linkers, which connect the two motor domains and can undergo a docking/undocking transition,…

生物大分子 · 定量生物学 2015-05-27 András Czövek , Gergely J Szöllősi , Imre Derényi

Recently individual two-headed kinesin molecules have been studied in in vitro motility assays revealing a number of their peculiar transport properties. In this paper we propose a simple and robust model for the kinesin stepping process…

统计力学 · 物理学 2009-10-31 Imre Derenyi , Tamas Vicsek

Non-processive molecular motors have to work together in ensembles in order to generate appreciable levels of force or movement. In skeletal muscle, for example, hundreds of myosin II molecules cooperate in thick filaments. In non-muscle…

生物物理 · 物理学 2015-06-16 Thorsten Erdmann , Philipp J. Albert , Ulrich S. Schwarz

A model for the processive movement of dynein is presented based on experimental observations available. In the model, the change from strong microtubule-binding to weak binding of dynein is determined naturally by the variation of the…

生物大分子 · 定量生物学 2007-05-23 Ping Xie , Shuo-Xing Dou , Peng-Ye Wang

We investigate the isometric transient response of muscle using a quantitative stochastic model of the actomyosin cycle based on the swinging lever-arm hypothesis. We first consider a single pair of filaments, and show that when values of…

生物物理 · 物理学 2009-11-10 Andrej Vilfan , Thomas Duke

The collective dynamics of $N$ weakly coupled processive molecular motors are considered theoretically. We show, using a discrete lattice model, that the velocity-force curves strongly depend on the effective dynamic interactions between…

亚细胞过程 · 定量生物学 2009-11-11 O. Campas , Y. Kafri , K. B. Zeldovich , J. Casademunt , J. -F. Joanny

We consider a model of an extensible semiflexible filament moving in two dimensions on a motility assay of motor proteins represented explicitly as active harmonic linkers. Their heads bind stochastically to polymer segments within a…

生物物理 · 物理学 2021-08-31 Amir Shee , Nisha Gupta , Abhishek Chaudhuri , Debasish Chaudhuri

Myosin II isoforms with varying mechanochemistry and filament size interact with filamentous actin (F-actin) networks to generate contractile forces in cells. How their properties control force production in environments with varying…

亚细胞过程 · 定量生物学 2014-07-09 Samantha Stam , Jon Alberts , Margaret L. Gardel , Edwin Munro

In cells, organelles and vesicles are usually transported by cooperation of several motor proteins, including plus-end directed motor kinesin and minus-end directed motor dynein. Many biophysical models have been constructed to understand…

化学物理 · 物理学 2015-05-19 Yunxin Zhang

In this study, through phenomenological comparison of the velocity-force data of processive motor proteins, including conventional kinesin, cytoplasmic dynein and myosin V, we found that, the ratio between motor velocities of two different…

生物物理 · 物理学 2015-05-30 Yunxin Zhang

We consider the dynamics of a rigid filament in a motor protein assay under external loading. The motor proteins are modeled as active harmonic linkers with tail ends immobilized on a substrate. Their heads attach to the filament…

生物物理 · 物理学 2021-12-23 Amir Shee , Subhadip Ghosh , Debasish Chaudhuri

We model and simulate the stepping dynamics of the kinesin motor including electric and mechanical forces, environmental noise, and the complicated potentials produced by tracking and neighboring protofilaments. Our dynamical model supports…

生物物理 · 物理学 2016-05-02 Alexander I Nesterov , Gennady P Berman , Mónica F Ramírez

Here we generalize our previous model of molecular motors trafficking subdiffusing cargos in viscoelastic cytosol by (i) including mechanochemical coupling between cyclic conformational fluctuations of the motor protein driven by the…

生物物理 · 物理学 2015-05-01 Igor Goychuk

The dynamics of motor protein molecules that have two subunits is investigated using simple discrete stochastic models. Exact steady-state analytical expressions are obtained for velocities and dispersions for any number of intermediate…

软凝聚态物质 · 物理学 2015-06-25 Anatoly B. Kolomeisky , Hubert Phillips

The human arm exhibits remarkable capabilities, including both explosive power and precision, which demonstrate dexterity, compliance, and robustness in unstructured environments. Developing robotic systems that emulate human-like…

机器人学 · 计算机科学 2025-11-11 Jianbo Yuan , Jing Dai , Yerui Fan , Yaxiong Wu , Yunpeng Liang , Weixin Yan

We propose a two-dimensional model for a complete description of the dynamics of molecular motors, including both the processive movement along track filaments and the dissociation from the filaments. The theoretical results on the…

生物大分子 · 定量生物学 2009-11-10 Ping Xie , Shuo-Xing Dou , Peng-Ye Wang