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• W1966974907 abstract "Monolayers of gramicidin A, pure and in mixtures with dimyristoylphosphatidylcholine (DMPC), were studied in situ at the air/H2O and air/D2O interfaces by polarization-modulated infrared reflection absorption spectroscopy (PM-IRRAS). Simulations of the entire set of amide I absorption modes were also performed, using complete parameter sets for different conformations based on published normal mode calculations. The structure of gramicidin A in the DMPC monolayer could clearly be assigned to a β6.3 helix. Quantitative analysis of the amide I bands revealed that film pressures of up to 25–30 mN/m the helix tilt angle from the vertical in the pure gramicidin A layer exceeded 60°. A marked dependence of the peptide orientation on the applied surface pressure was observed for the mixed lipid-peptide monolayers. At low pressure the helix lay flat on the surface, whereas at high pressures the helix was oriented almost parallel to the surface normal." @default.
• W1966974907 created "2016-06-24" @default.
• W1966974907 creator A5039484623 @default.
• W1966974907 creator A5040027813 @default.
• W1966974907 date "1999-03-01" @default.
• W1966974907 modified "2023-10-12" @default.
• W1966974907 title "Polarization-Modulated FTIR Spectroscopy of Lipid/Gramicidin Monolayers at the Air/Water Interface" @default.
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• W1966974907 doi "https://doi.org/10.1016/s0006-3495(99)77323-6" @default.
• W1966974907 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1300140" @default.
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