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- W2040384181 abstract "The conformational and spatial configuration of the biologically active undecapeptide physalaemin was studied using 350-MHz 1H NMR. The NMR analyses suggested the existence of a strong hydrogen bond between the amide proton of the Phe7 and a carbonyl group in the N-terminal moiety, most likely the Pro4 one. Other bondings were postulated, involving the side-chain amine of Lys6 and the side-chain amide of Asn5 and respectively the side-chain carboxyl of Asp3 and the terminal amide carbonyl of Met-NH2. Thus unlike its shorter peptidic fragments, physalaemin exhibited a stable molecular structure in solution, giving some insight into the conformation required for interaction at the biological receptor of tachykinins." @default.
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- W2040384181 date "1984-07-01" @default.
- W2040384181 modified "2023-09-25" @default.
- W2040384181 title "Conformation of physalaemin" @default.
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- W2040384181 doi "https://doi.org/10.1111/j.1432-1033.1984.tb08297.x" @default.
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