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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

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Official URL: http://dx.doi.org/10.1080/08927020902974063

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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:
DateEvent
2009Published
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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