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Sequence-specific 1h nmr assignments and secondary structure of neuropeptide y analogs in aqueous solution



Solution structures of neuropeptide Y analogs NP158 and NP181 were studied by 1H NMR spectroscopy. Sequential assignments were made at pH 3.5 at 25°C and 45°C using COSY, HOHAHA and ROESY spectra. Modeling shows turn-type loop structures in aqueous solution that could be important for receptor binding and/or antagonistic potency.. No significant conformational differences were observed between the two polypeptides despite vastly different antagonistic potency towards NPY YI receptors.
