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Structure of Leu5-enkephalin bound to a model membrane as determined by high-resolution NMR

✍ Scribed by Charles R. Watts; Michael R. Tessmer; Deborah A. Kallick

Publisher
Springer Netherlands
Year
1995
Tongue
English
Weight
826 KB
Volume
2
Category
Article
ISSN
1573-3149

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✦ Synopsis

Opioid peptides are thought to interact with the cell membrane in their biological journey to the membranebound receptor. Both organic solvents and model membranes have been used previously to determine the stable solution conformations of peptide hormones. Leucine enkephalin has been studied in a number of different environments, but with limited resolution. Here it is shown that leucine enkephalin forms a stable type IV [3-turn structure in dodecylphosphocholine micelles. We have observed a highly solvent-shielded amide proton with no evidence for a complementary hydrogen bond acceptor. The structural details of the peptide as determined by NMR spectroscopy in solution are described.

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