The three dimensional structure of eel calcitonin and two glycosolated derivatives was determined in micelles using solution NMR techniques and in oriented bilayers using solid-state NMR. The peptides were found to contain an alpha-helical stretch across most of the peptide with an unstructured carboxy terminal end. The glycosolation had little influence on the conformation of the peptide. The dynamic fluctuations of the backbone where however constrained somewhat by the presence of the carbohydrate groups. The peptide was labeled synthetically with 15N leu in the middle of the helical stretch. Solid-state NMR measurements were made of the peptide incorporated into lipid bilayers oriented on glass plates. The 15N chemical shift spectrum indicated a frequency in the region of the 15N chemical shift anisotropy tensor that represents a helical orientation perpendicular to the bilayer normal. The orientation of the helix was determined to lie in the plane of the bilayer in the native peptide as well as the glycosolated derivatives. The glycolslation did not effect the overall topology of the peptide.
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