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Three-color single-molecule imaging reveals conformational dynamics of dynein undergoing motility
[article]
2020
bioRxiv
pre-print
The motor protein dynein undergoes coordinated conformational changes of its domains during motility along microtubules. Previous single-molecule studies analyzed the motion of the AAA rings of the dynein homodimer, but not the distal microtubule binding domains (MTBD) that step along the track. Here, we simultaneously tracked two MTBDs and one AAA ring of a single dynein, as it undergoes hundreds of steps with nanometer precision using three-color imaging. We show that the AAA ring and the
doi:10.1101/2020.12.20.423706
fatcat:42tze7echrb5tiq4nxjpazw2za