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• W2000959507 abstract "The solution structure of human neuropeptide Y has been solved by conventional two-dimensional NMR techniques followed by distance-geometry and molecular-dynamics methods. The conformation obtained is composed of two short contiguous α-helices comprising residues 15–26 and 28–35, linked by a hinge inducing a 100° angle. The first helix (15–26) is connected to a polyproline stretch (residues 1–10) by a tight hairpin (residues 11–14). The helices and the polyproline stretch are packed together by hydrophobic interactions. This structure is related to that of the homologous avian pancreatic polypeptide and bovine pancreatic polypeptide. The C- and N-terminii, known to be involved in the biological activity for respectively the receptor binding and activation, are close together in space. The side chains of residues Arg33, Arg35 and Tyr36 on the one hand, and Tyr1 and Pro2 on the other, form a continuous solvent-exposed surface of 4.9 nm2 which is supposed to interact with the receptor for neuropeptide Y." @default.
• W2000959507 created "2016-06-24" @default.
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• W2000959507 date "1992-10-01" @default.
• W2000959507 modified "2023-09-27" @default.
• W2000959507 title "Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics" @default.
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• W2000959507 doi "https://doi.org/10.1111/j.1432-1033.1992.tb17346.x" @default.
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