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Secondary structure simulations of twin-arginine signal peptides in different environments
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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 ISSN 0892-7022.
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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 | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QC Physics |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) > Biological Sciences ( -2010) Faculty of Science, Engineering and Medicine > Science > Chemistry |
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Journal or Publication Title: | Molecular Simulation | ||||
Publisher: | Taylor & Francis Inc. | ||||
ISSN: | 0892-7022 | ||||
Official Date: | 2009 | ||||
Dates: |
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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
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