EEG correlates of hypnotic susceptibility based upon fast Fourier power spectral analysis.

The purpose of the present study was to determine if there were differences between high and low hypnotic susceptible subjects based upon fast Fourier power spectral analysis of the EEG recorded both before and during hypnotic tasks from frontal-temporal and occipital-parietal locations. Significant differences were obtained based upon EEG recording electrode location, EEG frequency within six different frequency domains, and hypnotic tasks. However, no main effect differences were obtained based upon hypnotic susceptibility. In contrast to some evoked potential studies in which a few differences have been obtained based on hypnotic susceptibility the lack of any EEG differences in this study even when positive and negative hallucination tasks were employed may have implications for the role of the neocortex in mediating hypnotic phenomena.

Conformations of model peptides in membrane-mimetic environments.

The influence of a membrane environment on the conformational energetics of a polypeptide chain has been investigated through studies of model peptides in a variety of membrane-mimetic media. Nuclear magnetic resonance (NMR) and circular dichroism (CD) data have been obtained for the peptides in bulk hydrophobic solvents, normal micelles, and reversed micelles. Several hydrophobic peptides which are sparingly soluble in water have been solubilized in aqueous sodium dodecyl sulfate (SDS) solution. NMR and CD data indicate that the micelle-solubilized peptides experience an environment with the conformational impact of bulk methanol, and have decreased conformational freedom. The site of residence of the peptides interacting with the micelles appears to be near the surfactant head groups, in a region permeated by water, and not in the micelle core. Strongly hydrophilic peptides have been solubilized in nonpolar solvents by reversed micelles. These peptides are located in small water pools in close association with the head groups of the surfactant. NMR and CD data show that there is a conformational impact of this interfacial water region on peptide solubilizates distinct from that of bulk water.