Charged or aromatic anchor residue dependence of transmembrane peptide tilt.

  title={Charged or aromatic anchor residue dependence of transmembrane peptide tilt.},
  author={Vitaly V. Vostrikov and Anna E Daily and Denise V Greathouse and Roger E Koeppe},
  journal={The Journal of biological chemistry},
  volume={285 41},
The membrane-spanning segments of integral membrane proteins often are flanked by aromatic or charged amino acid residues, which may "anchor" the transmembrane orientation. Single spanning transmembrane peptides such as those of the WALP family, acetyl-GWW(LA)(n)LWWA-amide, furthermore adopt a moderate average tilt within lipid bilayer membranes. To understand the anchor residue dependence of the tilt, we introduce Leu-Ala "spacers" between paired anchors and in some cases replace the outer… CONTINUE READING
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Aromatic and Charged Membrane Anchors 31730 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

  • P. C. van der Wel, N. D. Reed, D. V. Greathouse, R. E. Koeppe
  • July 28,
  • 2010

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