Extended structures intramolecular potential functions

NMR spectroscopy is a well-suited technique to study the membrane interactions of antimicrobial peptides by taking advantage of the orientational dependence of nuclear spin interactions. This paper discusses several solid-state NMR experiments to extend information on the peptide structure and dynamics as well as on the effect of antimicrobial peptides on model membranes. More specifically, studies of peptide dynamics by and N CP/MAS and static experiments were reported. A set of orientational restraint potentials for solid-state NMR observables in-eluding N chemical shift and N- H dipolar coupling was developed. The N-H X (X = N,0,S) intramolecular hydrogen bond in the series of 2(2 -heteroaryl)pyrroles and their trifluoroacetyl derivatives was examined by the H, N spectroscopy and density functional theory (DFT)... 

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