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- Koeppe, Roger E., et al. Show all 6 Authors
- Biochemistry 2014 v.53 no.22 pp. 3637-3645
- amino acids; aromatic compounds; ethanol; hydrogen bonding; hydrophobicity; lipid bilayers; lipids; membrane proteins; nuclear magnetic resonance spectroscopy; peptides
- ... Aromatic amino acids often flank the transmembrane alpha helices of integral membrane proteins. By favoring locations within the membrane–water interface of the lipid bilayer, aromatic residues Trp, Tyr, and sometimes Phe may serve as anchors to help stabilize a transmembrane orientation. In this work, we compare the influence of interfacial Trp, Tyr, or Phe residues upon the properties of tilted ...
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