Sataric M V, Tuszynski J A
Faculty of Technical Sciences, University of Novi Sad, Novi Sad, Serbia 21 000 Serbia and Montenegro.
J Biol Phys. 2005 Dec;31(3-4):487-500. doi: 10.1007/s10867-005-7288-1.
A recently developed model of nonlinear dynamics for microtubules is further expanded based on the biophysical arguments involving the secondary structure of the constitutive protein tubulin and on the ferroelectric properties of microtubules. It is demonstrated that kink excitations arise due to GTP hydrolysis that causes a dynamical transition in the structure of tubulin. The presence of an intrinsic electric field associated with the structure of a microtubule leads to unidirectional propagation of the kink excitation along the microtubule axis. This mechanism offers an explanation of the dynamic instability phenomenon in terms of the electric field effects. Moreover, a possible elucidation of the unidirectional transport of cargo via motor proteins such as kinesin and dynein is proposed within the model developed in this paper.
基于涉及组成蛋白微管蛋白二级结构的生物物理论据以及微管的铁电特性,对最近开发的微管非线性动力学模型进行了进一步扩展。结果表明,由于GTP水解导致微管蛋白结构发生动态转变,从而产生扭结激发。与微管结构相关的固有电场的存在导致扭结激发沿微管轴单向传播。该机制从电场效应的角度解释了动态不稳定性现象。此外,本文所开发的模型还提出了一种可能的解释,即通过驱动蛋白和动力蛋白等马达蛋白实现货物单向运输的原因。