Polypeptide Liquid Crystals: A Deuterium NMR Study

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Abstract
In polypeptide liquid crystals deuterium NMR spectra of labeled guest molecules and labeled Polybenzylglutamate exhibit a characteristic doubling (anisochronism) of the quadrupolar splittings of enantiotopic deuterons. The anisochronism is a reflection of local chirality. For achiral guests the chirality is acquired in collision complexes with the chiral polypeptide. The labeled polypeptide results suggest that the observed anisochronism is related to specific sidechain secondary structures. The observations are consistent with a model of solvent and/or temperature compensation in these lyotropic cholesteric phases wherein a polypeptide sidechain conformational transition is invoked.