Structural determination of the vasoactive intestinal peptide by two-dimensional H-NMR spectroscopy.
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.
Theriault
Y
Y
Departement de chimie, Universite de Montreal, C.P. 6128, Succ. A, Montreal, Quebec H3C 3J7
Boulanger
Y
Y
St-Pierre
S
S
D000595:Amino Acid Sequence; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014660:Vasoactive Intestinal Peptide / Q000737:chemistry*
D014660:Vasoactive Intestinal Peptide