Structural determination of the vasoactive intestinal peptide by two-dimensional H-NMR spectroscopy.

Biopolymers

Departement de chimie, Universite de Montreal, C.P. 6128, Succ. A, Montreal, Quebec H3C 3J7

Published: March 1991

The structure of the vasoactive intestinal peptide 1-28 in 40% 2,2,2-trifluoroethanol was investigated by two-dimensional 1H-nmr spectroscopy. All 1H resonances, except the gamma, delta, and epsilon protons of the lysine residues, could be sequentially assigned. Numerous intraresidual as well as short-range interresidual nuclear Overhauser effect spectroscopy connectivities were observed. Using a variable-target function minimization, a molecular model consisting of two helical stretches involving residues 7-15 and 19-27 connected by a region of undefined structure was calculated. The existence of an undefined structure between residues 16 and 18 confers mobility to the peptide molecule.

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http://dx.doi.org/10.1002/bip.360310411DOI Listing

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