We have demonstrated compression stress induced mechanical deformation of microtubules (MTs) on a two-dimensional elastic medium and investigated the role of compression strain, strain rate, and a MT-associated protein in the deformation of MTs. We show that MTs, supported on a two-dimensional substrate by a MT-associated protein kinesin, undergo buckling when they are subjected to compression stress. Compression strain strongly affects the extent of buckling, although compression rate has no substantial effect on the buckling of MTs. Most importantly, the density of kinesin is found to play the key role in determining the buckling mode of MTs. We have made a comparison between our experimental results and the ‘elastic foundation model’ that theoretically predicts the buckling behavior of MTs and its connection to MT-associated proteins. Taking into consideration the role of kinesin in altering the mechanical property of MTs, we are able to explain the buckling behavior of MTs by the elastic foundation model. This work will help understand the buckling mechanism of MTs and its connection to MT-associated proteins or surrounding medium, and consequently will aid in obtaining a meticulous scenario of the compression stress induced deformation of MTs in cells.
Water structure modification by urea and temperature has been studied in aqueous solution by analyses of changes in hydrogen bonding and extent of aggregation. ABSTRACT Water absorption peaks in near-infrared (NIR) and attenuated total reflectance (ATR)-Fourier transform infrared (FTIR), spectroscopy at different temperatures both in the absence and presence of urea have been analyzed to investigate hydrogen bonding in aqueous solution by perturbations of temperatures and concentration of urea. Concentration dependent basic spectra of aqueous urea solutions represent different clusters in the system originated from the difference of the extent of self-aggregation of urea molecules and water-urea interactions. Derivative and deconvoluted spectra confirm the presence of different structural components or clusters in pure water; but in presence of urea a new strong water cluster could be identified for the first time after certain concentration of urea. The degree of perturbation has been evaluated by 2D correlation and difference spectroscopy. Apparent molar volume, free energy change of activation (∆G), change in enthalpy of activation (∆H) and entropy of activation (∆S) for viscous flow of water in presence and absence of urea have been analyzed. The comprehensive analyses help to infer different extent of aggregation of urea molecules and formation of clusters by water-urea interactions in aqueous urea solutions.
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