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*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

8 Citations (Scopus)
217 Downloads (Pure)


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.

Original languageEnglish
Pages (from-to)1096-1102
Number of pages7
JournalACS Synthetic Biology
Issue number6
Early online date21 Feb 2017
Publication statusPublished - 16 Jun 2017

Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute

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