Association of neighboring β-strands of outer membrane protein A in lipid bilayers revealed by site-directed fluorescence quenching.

@article{Kleinschmidt2011AssociationON,
  title={Association of neighboring $\beta$-strands of outer membrane protein A in lipid bilayers revealed by site-directed fluorescence quenching.},
  author={J. Kleinschmidt and Paula V. Bulieris and J. Qu and M. Dogterom and T. den Blaauwen},
  journal={Journal of molecular biology},
  year={2011},
  volume={407 2},
  pages={
          316-32
        }
}
We present a detailed study on the formation of neighboring β-strands during the folding of a monomeric integral membrane protein of the β-barrel type. β-Strand and β-barrel formations were investigated for the eight-stranded transmembrane domain of outer membrane protein A (OmpA) with single-tryptophan (W), single-cysteine (C) OmpA mutants. Based on the OmpA structure, W and C were introduced in two neighboring β-strands oriented toward the hydrocarbon core of the membrane. Replaced residue… Expand
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