Earlier obtained two-dimensional ~H-NMR spectroscopy
data were used to analyze the spatial structure and conformational mobility of the double right TI 1rlr7~ helix of the complex formed by gramicidine A and Cs ÷ ions in an organic solvent (a chloroform-methanol mixture). Analysis of the experimental data permitted the determination of a set of conformations for each of the high-mobility residue side chains in the solution. The energy refinement of the most probable conformation of the double
right 11 ~'Tr7L.2o helix was made and conformational rearrangements of the tryptophan residue side chain were studied in detail.
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