Construction of a Chassis for a Tripartite Protein-Based Molecular Motor.

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

ACS synthetic biology 2017 Jun 16

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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 antiparallel 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 structure designed 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

Lara S R Small, Marc Bruning, Andrew R Thomson, Aimee L Boyle, Roberta B Davies, Paul M G Curmi, Nancy R Forde, Heiner Linke, Derek N Woolfson, Elizabeth H C Bromley. Construction of a Chassis for a Tripartite Protein-Based Molecular Motor. ACS synthetic biology. 2017 Jun 16;6(6):1096-1102