Young J J, Jung L J, Liu W T, Ho S N, Chang L R, Tsai Y C, Bhaskaran R, Yu C
Institute of Preventive Medicine, National Defence Medical Center, Taipei, Taiwan, R.O.C.
J Antibiot (Tokyo). 1994 Aug;47(8):922-31. doi: 10.7164/antibiotics.47.922.
Studies on the solution conformation of the cyclic depsipeptide antibiotic enopeptin A have been carried out using 2D NMR and molecular modelling techniques. The proton resonances of the antibiotic in DMSO-d6 have been assigned by the use of TOCSY and ROESY experiments. The interproton distance information obtained from the ROESY experiments have been used as the basis for elucidating the probable structures in solution. The restrained molecular dynamics technique was applied to calculate the structures in solution, and six resultant structures with fewer distance constraint violations were obtained that satisfy the experimental restraints very well. The conformation of the cyclic moiety of the molecules is well defined whereas the aliphatic chain segment is disordered.
已使用二维核磁共振（2D NMR）和分子建模技术对环缩肽抗生素恩诺肽A的溶液构象进行了研究。通过全相关谱（TOCSY）和旋转坐标系中的核Overhauser效应谱（ROESY）实验确定了抗生素在氘代二甲亚砜（DMSO-d6）中的质子共振。从ROESY实验获得的质子间距离信息已被用作阐明溶液中可能结构的基础。应用受限分子动力学技术计算溶液中的结构，得到了六个距离约束违反较少的结构，这些结构很好地满足了实验约束。分子环部分的构象明确，而脂肪链段无序。
