Molecular Ordering of Interfacially Localized Tryptophan Analogs in Ester- and Ether-Lipid Bilayers Studied by 2H-NMR

This publication has 33 references indexed in Scilit:

• The Cation−π Interaction
  Chemical Reviews, 1997
• Conformation of micellar phospholipid bound to the active site of phospholipase A2
  Biochemistry, 1995
• Orientations of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy
  Biophysical Journal, 1994
• Tryptophans in membrane proteins: Indole ring orientations and functional implications in the gramicidin channel
  Biochemistry, 1993
• Partitioning of tryptophan side-chain analogs between water and cyclohexane
  Biochemistry, 1992
• Hydrogen bond stereochemistry in protein structure and function
  Journal of Molecular Biology, 1990
• The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices
  Biochemistry, 1989
• Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution
  Biochemistry, 1988
• Ether phosphatidylcholines: comparison of miscibility with ester phosphatidylcholines and sphingomyelin, vesicle fusion, and association with apolipoprotein A-I
  Biochemistry, 1986
• The Use of Phase-Transfer Catalysis for theN-Alkylation of Indole
  Synthesis, 1976