Molecular Crystals and Liquid Crystals, Vol.465, 133-141, 2007
Conformation and orientation of an oligopeptide in a lyotropic mesophase by H-1 NMR
The analysis of H-1 residual dipolar couplings of zwitterionic tetraalanine in the lyotropic system cesium pentadecafluorooctanoate in water (CsPFO/D2O) showed that the internal peptide residues adopt a polyproline II helix conformation. Moreover, the data allowed an estimate of the dihedral angles of the external residues and suggested that the long molecular axis is tilted by an angle of 56 degrees with respect to the surface of the micelles formed by CsPFO.
Keywords:conformation;liquid crystal NMR;orientation;residual dipolar couplings;zwitterionic tetraalanine