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| Content Provider | PubMed Central |
|---|---|
| Author | Lavoie, Hugo Daniel, Blaudez Vaknin, David Bernard, Desbat Ocko, Benjamin M. Christian, Salesse |
| Abstract | Monomolecular films of valine gramicidin A (VGA) were investigated in situ at the air-water interface by x-ray reflectivity and x-ray grazing incidence diffraction as well as polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS). These techniques were combined to obtain information on the secondary structure and the orientation of VGA and to characterize the shoulder observed in its pi-A isotherm. The thickness of the film was obtained by x-ray reflectivity, and the secondary structure of VGA was monitored using the frequency position of the amide I band. The PM-IRRAS spectra were compared with the simulated ones to identify the conformation adopted by VGA in monolayer. At large molecular area, VGA shows a disordered secondary structure, whereas at smaller molecular areas, VGA adopts an anti-parallel double-strand intertwined beta(5.6) helical conformation with 30 degrees orientation with respect to the normal with a thickness of 25 A. The interface between bulk water and the VGA monolayer was investigated by x-ray reflectivity as well as by comparing the experimental and the simulated PM-IRRAS spectra on D(2)O and H(2)O, which suggested the presence of oriented water molecules between the bulk and the monolayer. |
| Starting Page | 3558 |
| File Format | |
| ISSN | 15420086 |
| e-ISSN | 15420086 |
| Journal | Biophysical Journal |
| Issue Number | 6 |
| Volume Number | 83 |
| Language | English |
| Publisher Date | 2002-12-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biophysics |
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