Published March 10, 2006
| Supplemental Material
Journal Article
Open
Engineering Cooperativity in Biomotor-Protein Assemblies
Abstract
A biosynthetic approach was developed to control and probe cooperativity in multiunit biomotor assemblies by linking molecular motors to artificial protein scaffolds. This approach provides precise control over spatial and elastic coupling between motors. Cooperative interactions between monomeric kinesin-1 motors attached to protein scaffolds enhance hydrolysis activity and microtubule gliding velocity. However, these interactions are not influenced by changes in the elastic properties of the scaffold, distinguishing multimotor transport from that powered by unorganized monomeric motors. These results highlight the role of supramolecular architecture in determining mechanisms of collective transport.
Additional Information
© 2006 American Association for the Advancement of Science. 2 November 2005; Accepted 6 February 2006. We thank A. J. Link and I. Fushman their help during the early stages of this project; L. Wade and D. Pearson for use of the temperature controller; and P. Wiggins, R. Bao, T. Squires, and S. Quake for valuable discussions. This work was supported by the Beckman Foundation through a Beckman Senior Research Fellowship (to M.R.D.) and by a grant from the National Science Foundation.Attached Files
Supplemental Material - Diehl_SOM.pdf
Files
Diehl_SOM.pdf
Files
(120.1 kB)
| Name | Size | Download all |
|---|---|---|
|
md5:721aae3bac80b3cc24f4df16965d4933
|
120.1 kB | Preview Download |
Additional details
- Eprint ID
- 52025
- Resolver ID
- CaltechAUTHORS:20141120-161852368
- Arnold and Mabel Beckman Foundation
- NSF
- Created
-
2014-11-21Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field