The Library
Secondary structure simulations of twin-arginine signal peptides in different environments
Tools
Tools
Tools
San-Miguel, Miguel A., Robinson, Colin and Rodger, P. Mark (2009) Secondary structure simulations of twin-arginine signal peptides in different environments. Molecular Simulation, Vol.35 (No.12-13). pp. 1033-1042. doi:10.1080/08927020902974063
Research output not available from this repository, contact author.
Official URL: http://dx.doi.org/10.1080/08927020902974063
Abstract
The twin-arginine translocation (Tat) system transports folded proteins across bacterial plasma membranes and the chloroplast thylakoid membrane. A twin-arginine motif in the signal peptide sequence plays a key role in the signal process. In this article we report the results of molecular dynamics simulations on a typical Escherichia coli RR-signal peptide and two mutant variants in both aqueous and trifluoroethanol (TFE) solutions. It has been found that the peptide switches between two distinct states: random coil in water and some helical content in TFE. Our simulations demonstrate that the wild-type peptide is considerably more flexible than either of the mutants in both the solvents investigated. The twin-arginine motif was found to provide a nucleation point for the formation of an -helix in water, but also appears to destabilise -helices in other regions of the peptide when dissolved in TFE.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QC Physics |
||||
| Divisions: | Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010) Faculty of Science > Chemistry |
||||
| Journal or Publication Title: | Molecular Simulation | ||||
| Publisher: | Taylor & Francis Inc. | ||||
| ISSN: | 0892-7022 | ||||
| Official Date: | 2009 | ||||
| Dates: |
|
||||
| Volume: | Vol.35 | ||||
| Number: | No.12-13 | ||||
| Number of Pages: | 10 | ||||
| Page Range: | pp. 1033-1042 | ||||
| DOI: | 10.1080/08927020902974063 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | Engineering and Physical Sciences Research Council (EPSRC) | ||||
| Grant number: | GR/R36503 |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
