Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments.

@article{Rizo1993ConformationalBO,
  title={Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments.},
  author={Josep Rizo and Francisco J Blanco and Bostjan Kobe and Martha D Bruch and Lila M. Gierasch},
  journal={Biochemistry},
  year={1993},
  volume={32 18},
  pages={4881-94}
}
Nuclear magnetic resonance and circular dichroism (CD) studies of isolated peptides corresponding to WT and mutant OmpA signal sequences are reported; all of the peptides adopt substantial amounts of alpha-helical structure both in 1:1 (v/v) trifluoroethanol (TFE)/water and in sodium dodecyl sulfate (SDS) micelles. In TFE/water, the helix begins after the positively charged N-terminal residues and is most stable in the hydrophobic core, which correlates with results obtained previously for… CONTINUE READING

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