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- W1539364025 abstract "Dermorphin has been studied in various solvents (DMSO, TFE and $H_2$O) using spectroscopic techniques such as CD and NMR. Potential energy minimization of the peptide structure has been carried out to verify the indications obtained from the spectroscopic data. All the results suggest the existence of a $ beta$-bend involving the central and carboxy-terminal part of the molecule. These findings could give reason of the behavior of the peptide in the presence of lipid moieties, where only a slight interaction is observed." @default.
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- W1539364025 date "1991-01-01" @default.
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- W1539364025 title "Conformation of dermorphin in solution and in the presence of lipids" @default.
- W1539364025 hasPublicationYear "1991" @default.
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