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Title: Dynamic Assembly of Polymer Nanotube Networks via Kinesin-Powered Microtubule Filaments.


Abstract not provided.

Publication Date:
Research Org.:
Sandia National Lab. (SNL-NM), Albuquerque, NM (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
Report Number(s):
DOE Contract Number:
Resource Type:
Resource Relation:
Conference: Proposed for presentation at the German-American Frontiers of Engineering Symposium held April 16-18, 2015 in Pottsdam, Germany.
Country of Publication:
United States

Citation Formats

Paxton, Walter F. Dynamic Assembly of Polymer Nanotube Networks via Kinesin-Powered Microtubule Filaments.. United States: N. p., 2015. Web.
Paxton, Walter F. Dynamic Assembly of Polymer Nanotube Networks via Kinesin-Powered Microtubule Filaments.. United States.
Paxton, Walter F. 2015. "Dynamic Assembly of Polymer Nanotube Networks via Kinesin-Powered Microtubule Filaments.". United States. doi:.
title = {Dynamic Assembly of Polymer Nanotube Networks via Kinesin-Powered Microtubule Filaments.},
author = {Paxton, Walter F},
abstractNote = {Abstract not provided.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = 2015,
month = 4

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  • In this study, we describe for the first time how biological nanomotors may be used to actively self-assemble mesoscale networks composed of diblock copolymer nanotubes. The collective force generated by multiple kinesin nanomotors acting on a microtubule filament is large enough to overcome the energy barrier required to extract nanotubes from polymer vesicles comprised of poly(ethylene oxide-b-butadiene) in spite of the higher force requirements relative to extracting nanotubes from lipid vesicles. Nevertheless, large-scale polymer networks were dynamically assembled by the motors. These networks displayed enhanced robustness, persisting more than 24 h post-assembly (compared to 4–5 h for corresponding lipid networks).more » The transport of materials in and on the polymer membranes differs substantially from the transport on analogous lipid networks. Specifically, our data suggest that polymer mobility in nanotubular structures is considerably different from planar or 3D structures, and is stunted by 1D confinement of the polymer subunits. Moreover, quantum dots adsorbed onto polymer nanotubes are completely immobile, which is related to this 1D confinement effect and is in stark contrast to the highly fluid transport observed on lipid tubules.« less
  • Abstract not provided.
  • Abstract not provided.
  • The assembly of microtubule-based cellular structures depends on regulated tubulin polymerization and directional transport. In this research, we have purified and characterized tubulin heterodimers that have human β-tubulin isotype III (TUBB3), as well as heterodimers with one of two β-tubulin mutations (D417H or R262H). Both point mutations are proximal to the kinesin-binding site and have been linked to an ocular motility disorder in humans. Compared to wild-type, microtubules with these mutations have decreased catastrophe frequencies and increased average lifetimes of plus- and minus-end-stabilizing caps. Importantly, the D417H mutation does not alter microtubule lattice structure or Mal3 binding to growing filaments.more » Instead, this mutation reduces the affinity of tubulin for TOG domains and colchicine, suggesting that the distribution of tubulin heterodimer conformations is changed. Together, our findings reveal how residues on the surface of microtubules, distal from the GTP-hydrolysis site and inter-subunit contacts, can alter polymerization dynamics at the plus- and minus-ends of microtubules.« less