Construction of a Chassis for a Tripartite Protein-Based Molecular Motor
(2017) In ACS Synthetic Biology 6(6). p.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 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... (More)
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.
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- author
- Small, Lara S.R.
; Bruning, Marc
; Thomson, Andrew R.
; Boyle, Aimee L.
; Davies, Roberta B.
; Curmi, Paul M G
; Forde, Nancy R.
; Linke, Heiner
LU
; Woolfson, Derek N and Bromley, Elizabeth H. C.
- organization
- publishing date
- 2017-06-16
- type
- Contribution to journal
- publication status
- published
- subject
- in
- ACS Synthetic Biology
- volume
- 6
- issue
- 6
- pages
- 7 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000403864900019
- pmid:28221767
- scopus:85020892104
- ISSN
- 2161-5063
- DOI
- 10.1021/acssynbio.7b00037
- language
- English
- LU publication?
- yes
- id
- 83db0976-983d-45df-9993-8da024db8617
- date added to LUP
- 2017-07-04 08:27:55
- date last changed
- 2025-01-07 16:35:11
@article{83db0976-983d-45df-9993-8da024db8617, abstract = {{<p>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.</p>}}, author = {{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.}}, issn = {{2161-5063}}, language = {{eng}}, month = {{06}}, number = {{6}}, pages = {{1096--1102}}, publisher = {{The American Chemical Society (ACS)}}, series = {{ACS Synthetic Biology}}, title = {{Construction of a Chassis for a Tripartite Protein-Based Molecular Motor}}, url = {{http://dx.doi.org/10.1021/acssynbio.7b00037}}, doi = {{10.1021/acssynbio.7b00037}}, volume = {{6}}, year = {{2017}}, }