ID: q-bio/0610045

Kinesin as an electrostatic machine

October 24, 2006

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The relevance of neck linker docking in the motility of kinesin

April 21, 2008

86% Match
Andras Czovek, Gergely J. Szollosi, Imre Derenyi
Biological Physics
Biomolecules

Conventional kinesin is a motor protein, which is able to walk along a microtubule processively. The exact mechanism of the stepping motion and force generation of kinesin is still far from clear. In this paper we argue that neck linker docking is a crucial element of this mechanism, without which the experimentally observed dwell times of the steps could not be explained under a wide range of loading forces. We also show that the experimental data impose very strict constrai...

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A Brownian Dynamics Model of Kinesin in Three Dimensions Incorporating the Force-Extension Profile of the Coiled-Coil Cargo Tether

October 29, 2009

86% Match
P. J. Atzberger, C. S. Peskin
Soft Condensed Matter
Statistical Mechanics
Biological Physics
Biomolecules

The Kinesin family of motor proteins are involved in a variety of cellular processes that transport materials and generate force. With recent advances in experimental techniques, such as optical tweezers which can probe individual molecules, there has been an increasing interest in understanding the mechanisms by which motor proteins convert chemical energy into mechanical work. Here we present a mathematical model for the chemistry and three dimensional mechanics of the Kine...

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Motor Proteins Have Highly Correlated Brownian Engines

June 10, 1998

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G. P. Tsironis, K. Lindenberg
Statistical Mechanics

Two headed motor proteins, such as kinesin and dynein, hidrolyze environmental ATP in order to propel unidirectionally along cytoskeletal filaments such as microtubules. In the case of kinesin, protein heads bind primarily on the alpha tubulin site of asymmetric alpha-beta 8nm-long tubulin dimers that constitute the microtubular protofilaments. Kinesin dimers overcome local binding forces up to 5pN and are known to move on protofilaments with ATP concentration-dependent speed...

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Traffic of single-headed motor proteins KIF1A: effects of lane changing

December 28, 2007

86% Match
Debashish IITK Chowdhury, Ashok IITK Garai, Jian-Sheng NUS Wang
Biological Physics
Statistical Mechanics
Subcellular Processes

KIF1A kinesins are single-headed motor proteins which move on cylindrical nano-tubes called microtubules (MT). A normal MT consists of 13 protofilaments on which the equispaced motor binding sites form a periodic array. The collective movement of the kinesins on a MT is, therefore, analogous to vehicular traffic on multi-lane highways where each protofilament is the analogue of a single lane. Does lane-changing increase or decrease the motor flux per lane? We address this fun...

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Cooperative Protofilament Switching Emerges from Inter-Motor Interference in Multiple-Motor Transport

October 1, 2016

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David Ando, Michelle K. Mattson, ... , Gopinathan Ajay
Biomolecules
Subcellular Processes

Within living cells, the transport of cargo is accomplished by groups of molecular motors. Such collective transport could utilize mechanisms which emerge from inter-motor interactions in ways that are yet to be fully understood. Here we combined experimental measurements of two-kinesin transport with a theoretical framework to investigate the functional ramifications of inter-motor interactions on individual motor function and collective cargo transport. In contrast to kines...

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Microtubule Defects Influence Kinesin-Based Transport In Vitro

October 4, 2016

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Winnie H. Liang, Qiaochu Li, K. M. Rifat Faysal, Stephen J. King, ... , Xu Jing
Biomolecules
Subcellular Processes

Microtubules are protein polymers that form "molecular highways" for long-range transport within living cells. Molecular motors actively step along microtubules to shuttle cellular materials between the nucleus and the cell periphery; this transport is critical for the survival and health of all eukaryotic cells. Structural defects in microtubules exist, but whether these defects impact molecular motor-based transport remains unknown. Here, we report a new, to our knowledge, ...

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The kinesin walk: a dynamic model with elastically coupled heads

September 14, 1998

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Imre Derenyi, Tamas Vicsek
Statistical Mechanics

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 with elastically coupled Brownian heads showing all of these properties. The analytic and numerical treatment of our model results in a very good fit to the experimental data and practically has no free parameters. Changing the values of the ...

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Dynamics of heterodimeric kinesins and cooperation of kinesins

February 9, 2004

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Ping Xie, Shuo-Xing Dou, Peng-Ye Wang
Biomolecules

Using the model for the processive movement of a dimeric kinesin we proposed before, we study the dynamics of a number of mutant homodimeric and heterodimeric kinesins that were constructed by Kaseda et al. (Kaseda, K., Higuchi, H. and Hirose, K. PNAS 99, 16058 (2002)). The theoretical results of ATPase rate per head, moving velocity, and stall force of the motors show good agreement with the experimental results by Kaseda et al.: The puzzling dynamic behaviors of heterodimer...

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Crowding and pausing strongly affect dynamics of kinesin-1 motors along microtubules

May 9, 2018

85% Match
Matthias Rank, Erwin Frey
Biological Physics

Molecular motors of the kinesin-1 family move in a directed and processive fashion along microtubules (MTs). It is generally accepted that steric hindrance of motors leads to crowding effects; however, little is known about the specific interactions involved. We employ an agent-based lattice gas model to study the impact of interactions which enhance the detachment of motors from crowded filaments on their collective dynamics. The predictions of our model quantitatively agree...

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The intrinsic load-resisting capacity of kinesin

July 9, 2009

85% Match
Wenwei Zheng, Dagong Fan, ... , ZhisongWang
Biological Physics

Conventional kinesin is a homodimeric motor protein that is capable of walking unidirectionally along a cytoskeletal filament. While previous experiments indicated unyielding unidirectionality against an opposing load up to the so-called stall force, recent experiments also observed limited processive backwalking under superstall loads. This theoretical study seeks to elucidate the molecular mechanical basis for kinesin's steps over the full range of external loads that can p...

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