Theriault Y, Boulanger Y, St-Pierre S
Departement de chimie, Universite de Montreal, C.P. 6128, Succ. A, Montreal, Quebec H3C 3J7
Biopolymers. 1991 Mar;31(4):459-64. doi: 10.1002/bip.360310411.
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.
采用二维¹H-核磁共振光谱研究了血管活性肠肽1-28在40% 2,2,2-三氟乙醇中的结构。除赖氨酸残基的γ、δ和ε质子外，所有¹H共振峰均可进行顺序归属。观察到大量的残基内以及短程残基间的核Overhauser效应光谱相关性。通过可变目标函数最小化，计算出一个分子模型，该模型由两个螺旋片段组成，分别涉及7-15位残基和19-27位残基，中间由一段结构未明确的区域相连。16至18位残基间存在未明确结构，这赋予了肽分子一定的灵活性。
