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

Small, Lara S. R. and Bruning, Marc and Thomson, Andrew R. and Boyle, Aimee L. and Davies, Roberta B. and Curmi, Paul M. G. and Forde, Nancy R. and Linke, Heiner and Woolfson, Derek N. and Bromley, Elizabeth H. C. (2017) 'Construction of a chassis for a tripartite protein-based molecular motor.', ACS synthetic biology., 6 (6). pp. 1096-1102.

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.

Item Type:Article
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Status:Peer-reviewed
Publisher Web site:https://doi.org/10.1021/acssynbio.7b00037
Publisher statement:This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
Record Created:02 Mar 2017 09:59
Last Modified:20 Jun 2017 12:24

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