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.
FEBS Lett. 1995 vol. 371(1), pp. 35-38