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Structural determination of the vasoactive intestinal peptide by two‐dimensional 1 H‐nmr spectroscopy
Author(s) -
Theriault Y.,
Boulancer Y.,
StPierre S.
Publication year - 1991
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360310411
Subject(s) - chemistry , vasoactive intestinal peptide , nuclear magnetic resonance spectroscopy , peptide , spectroscopy , molecule , two dimensional nuclear magnetic resonance spectroscopy , crystallography , stereochemistry , nuclear magnetic resonance , organic chemistry , biochemistry , neuropeptide , receptor , physics , quantum mechanics
The structure of the vasoactive intestinal peptide 1–28 in 40% 2,2,2‐trifluoroethanol was investigated by two‐dimensional 1 H‐nmr spectroscopy. All 1 H resonances, except the γ, δ, and ε 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.