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Biophys J, December 2002, p. 3558-3569, Vol. 83, No. 6


*Département de Chimie-Biologie, Université du
Québec à Trois-Rivières, Trois-Rivières,
Québec G9A 5H7, Canada;
Centre de Physique
Moléculaire Optique et Hertzienne and §Laboratoire
de Physico-Chimie Moléculaire, Université Bordeaux I, 33405 Talence, France;
Ames Laboratory and Department of
Physics, Iowa State University, Ames, Iowa 50011 USA; and
¶Brookhaven National Laboratory, Department of Physics,
Upton, New York 11973 USA
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
-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
5.6 helical conformation with 30° orientation with
respect to the normal with a thickness of 25 Å. 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 D2O and H2O, which suggested the
presence of oriented water molecules between the bulk and the monolayer.
Biophys J, December 2002, p. 3558-3569, Vol. 83, No. 6
© 2002 by the Biophysical Society 0006-3495/02/12/3558/12 $2.00
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