Structural and conformational study of peptides containing glycine and alanine residues by 13C CPMAS NMR spectroscopy in solid state.

The results of the structural and conformational studies carried out using 13C CPMAS NMR technique on several glycine and alanine containing peptides in the solid state are reported. The study demonstrates the effects of variations in 13C chemical shifts due to conformation and hydrogen bonding. The possibility of applying this technique to obtain insight into the conformational characteristics of peptides of unknown structures is discussed.

Nuclear magnetic resonance and thermal studies of drug doped dipalmitoyl phosphatidyl choline-H2O systems.

The influence of the sulfone drugs, diamino diphenyl sulfone and diamino monophenyl sulfone on the phase transitions and dynamics of dipalmitoyl phosphatidyl choline-H2O/D2O vesicles have been investigated using differential scanning calorimetry and nuclear magnetic resonance. Our results show that diamino diphenyl sulfone interacts quite strongly with the headgroups of dipalmitoyl phosphatidyl choline whereas the diamino monophenyl sulfone-dipalmitoyl phosphatidyl choline interaction is quite weak. This is attributed to the difference in the structure and hydrophobic character of the two drugs.