ArticleBiophysical journal1999
Polarization-modulated FTIR spectroscopy of lipid/gramicidin monolayers at the air/water interface.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Article
- EHD2 restrains dynamics of caveolae by an ATP-dependent, membrane-bound, open conformation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Gramicidin A Channel Formation Induces Local Lipid Redistribution I: Experiment and Simulation.Biophysical journal · 2017Article
- Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins.Advances in colloid and interface science · 2014Review
- Infrared reflection-absorption spectroscopy: principles and applications to lipid-protein interaction in Langmuir films.Biochimica et biophysica acta · 2010Review
- Determination of the contribution of the myristoyl group and hydrophobic amino acids of recoverin on its dynamics of binding to lipid monolayers.Biophysical journal · 2007Article
- Facile lipid flip-flop in a phospholipid bilayer induced by gramicidin A measured by sum-frequency vibrational spectroscopy.Biophysical journal · 2007Article
- Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS).Biophysical journal · 2006Article
- Orientation and lipid-peptide interactions of gramicidin A in lipid membranes: polarized attenuated total reflection infrared spectroscopy and spin-label electron spin resonance.Biophysical journal · 2004Article
- Spectroscopic [correction of eSpectroscopic] and structural properties of valine gramicidin A in monolayers at the air-water interface.Biophysical journal · 2002Article
- Self-assembly of the hydrophobin SC3 proceeds via two structural intermediates.Protein science : a publication of the Protein Society · 2002Article
- Conducting gramicidin channel activity in phospholipid monolayers.Biophysical journal · 2001Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
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 beta6.3 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 degrees. 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.
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