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Paorunnan et al. previously showed that purified TFPs retain their functionality on liposomes but that their mechanical behavior is significantly altered. No corresponding study has been performed in small unilamellar vesicles(SUVs) of similar size. In this study, we comparatively probed the nanomechanical behavior of single TFP using total internal reflection fluorescence microscopy(TIRFM), atomic force microscopy(AFM) and microindentation techniques. We found that TFP formed robust structures with comparable mechanical properties to purified TFPs. Analysis of the TIRFM images yielded estimates of the vesicle relaxation time between 10-100s and yielded results that indicated that purified TFP first stiffens the liposome to micron-size dimensions and then flows, with the degree of bending dependent on theTFP retraction force. We also found that the TFP caused a measurable reduction in the vesicle stiffness though no fluidizing was observed. This was further verified by AFM analysis which showed that the direction of motion of the TFP resulted in rotational deformation of the liposome. In addition, AFM analysis showed that the sharpening of the contour lines as the TFP retracts corresponds to an increase in the apparent stiffness of the liposome, which was proportional to the amount of retraction force used. This reveals interesting experimental possibilities in the context of retraction based surface translocation and applications to nanomechanics.
To understand the nanoscale forces at the pump interface and their consequences for activity we have recently measured the force-extension properties of a single bacteriorhodopsin(BR) dimer using a single molecule pulldown assay. We isolated and quantified the forces on a BR dimer in a simple system for which the trans-membrane and cytoplasmic domains of the protein were also in solution. Our results revealed two distinct regimes: first, a low force regime, occurring close to the isometric point where the molecular weight of the protein roughly equals the weight of the dimer and second, a high force regime, in which the molecular weight is much greater than the weight of the dimer. Under low forces, a single pulling operation can cause either the dimer to break or the dimer does not break, with the probability of breaking roughly proportional to the force. d2c66b5586