Sunday, 1 June 2014

Intracellular dynamics probed with nanotubes

The movement of nanotube-labelled kinesin-1 motor proteins in cells was analysed using fluorescence microscopy.  At timeframes above 100 ms, researchers observed a regime of kinesin molecular motion different from thermal motion or directed motor activity.  In this regime, the kinesins were bound to the microtubule network, and moved randomly but remained locally constrained.  Their dynamics reflected nonequilibrium fluctuations in the microtubule network.  These fluctuations were driven by cytoplasmic myosin activity generating a random stirring effect. 

High-resolution mapping of intracellular fluctuations using carbon nanotubes; N. Fakhri et al; Science; Vol 344(6187); p 1031 

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