Discipline: Physics
Subcategory: Physics (not Nanoscience)
Angela V. Berry - Hampton University
Co-Author(s): Kun-Ta Wu, Brandeis University, Waltham, MA; Pooja Chandrakar, Brandeis University, Waltham, MA; Zvonimir Dogic, Brandeis University, Waltham, MA
Kinesins are molecular motor proteins that move along microtubules in eukaryotic cells. Kinesin 401 is a processive molecular motor that has two legs walking on a microtubule, whereas Kinesin 365 is a non-processive motor that has one leg, therefore hopping on a microtubule. When assembled into kinesin clusters, these motors convert ATP into ADP, driving microtubule network. Kinesins promote intracellular activity, but the role of their nano-scale stepping behaviors in micron-scale network activity remains unclear. Here, we synthesize an active gel, a network comprised of crosslinked microtubules driven by molecular motor clusters. The clusters are comprised of kinesin motors crosslinked by streptavidin. We measured the network activity driven by kinesins 401 and 365 when their concentration and the streptavidin concentration were varied. The results showed that K365 optimized microtubule activity. Our finding not only paves the way to outlining fundamental stepping behaviors of non-processive motors, but also sheds light on designing molecular motors that promote intracellular activity.
Not SubmittedFunder Acknowledgement(s): NSF MRSEC DMR 1420382
Faculty Advisor: Kun-Ta Wu, kwu@wpi.edu
Role: I conducted all of this research.