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Structural determination of the vasoactive intestinal peptide by two-dimensional 1H-nmr spectroscopy

✍ Scribed by Y. Theriault; Y. Boulancer; S. St-Pierre

Publisher: Wiley (John Wiley & Sons)
Year: 1991
Tongue: English
Weight: 443 KB
Volume: 31
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360310411

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✦ Synopsis

The structure of the vasoactive intestinal peptide 1-28 in 40% 2,2,2-trifluoroethanol was investigated by two-dimensional 'H-nmr spectroscopy. All 'H resonances, except the y, 6, and c 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.

' The helix propagation probability was found to be especially high for residues 13-20.8 Another

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