Construction of a chassis for a tripartite protein-based molecular motor

Small, Lara S.R.; Bruning, Marc; Thomson, Andrew R.; Boyle, Aimee L.; Davies, Roberta B.; Curmi, Paul M.G.; Forde, Nancy R.; Linke, Heiner; Woolfson, Derek N.; Bromley, Elizabeth H.C.

Abstract

Improving our understanding of biological motors, both to fully comprehend their activities in vital processes, and to exploit their impressive abilities for use in bionanotechnology, is highly desirable. One means of understanding these systems is through the production of synthetic molecular motors. We demonstrate the use of orthogonal coiled-coil dimers (including both parallel and anti-parallel coiled-coils) as a hub for linking other components of a previously described synthetic molecular motor, the Tumbleweed. We use circular dichroism, analytical ultracentrifugation, dynamic light scattering and disulfide rearrangement studies to demonstrate the ability of this six-peptide set to form the specific structure required for the Tumbleweed motor. The successful formation of a suitable hub structure is both a test of the transferability of design rules for protein folding as well as an important step in the production of a synthetic protein-based molecular motor.

Citation

Small, L. S., Bruning, M., Thomson, A. R., Boyle, A. L., Davies, R. B., Curmi, P. M., …Bromley, E. H. (2017). Construction of a chassis for a tripartite protein-based molecular motor. ACS Synthetic Biology, 6(6), 1096-1102. https://doi.org/10.1021/acssynbio.7b00037

• Journal Article Type: Article
• Acceptance Date: Feb 21, 2017
• Online Publication Date: Feb 21, 2017
• Publication Date: Feb 21, 2017
• Deposit Date: Feb 23, 2017
• Publicly Available Date: Mar 2, 2017
• Journal: ACS Synthetic Biology
• Publisher: American Chemical Society
• Peer Reviewed: Peer Reviewed
• Volume: 6
• Issue: 6
• Pages: 1096-1102
• DOI: https://doi.org/10.1021/acssynbio.7b00037
• Public URL: https://durham-repository.worktribe.com/output/1393032