Unfolding and extraction of a transmembrane alpha-helical peptide: dynamic force spectroscopy and molecular dynamics simulations.

@article{Contera2005UnfoldingAE,
  title={Unfolding and extraction of a transmembrane alpha-helical peptide: dynamic force spectroscopy and molecular dynamics simulations.},
  author={Sonia Antoranz Contera and Vincent Lema{\^i}tre and Maurits R R de Planque and Anthony Watts and John F. Ryan},
  journal={Biophysical journal},
  year={2005},
  volume={89 5},
  pages={
          3129-40
        }
}
An atomic force microscope (AFM) was used to visualize CWALP(19)23 peptides ((+)H(3)N-ACAGAWWLALALALALALALWWA-COO(-)) inserted in gel-phase DPPC and DSPC bilayers. The peptides assemble in stable linear structures and domains. A model for the organization of the peptides is given from AFM images and a 20 ns molecular dynamics (MD) simulation. Gold-coated AFM cantilevers were used to extract single peptides from the bilayer through covalent bonding to the cystein residue. Experimental and… CONTINUE READING

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