Palmer D E, Mierke D F, Pattaroni C, Goodman M, Wakamiya T, Fukase K, Kitazawa M, Fujita H, Shiba T
Biopolymers. 1989 Jan;28(1):397-408. doi: 10.1002/bip.360280137.
We report progress in elucidating the structure of nisin, a naturally occurring peptide antibiotic. Nisin contains five rings constrained by lanthionine or methyllanthionine bridges, as well as alpha, beta-unsaturated amino acids. We have determined conformations for two model compounds of ring A and a derivative of ring B through interactive nmr and computer simulation studies. High-resolution nmr techniques provides structural information, which was further refined through molecular dynamics simulations. These methods are being applied to the remaining constrained fragments of the molecule. This conformational information will be employed in an aufbau approach to determining the structure of the entire molecule.
我们报告了在阐明乳链菌肽（一种天然存在的肽抗生素）结构方面取得的进展。乳链菌肽含有由羊毛硫氨酸或甲基羊毛硫氨酸桥以及α,β-不饱和氨基酸所限制的五个环。我们通过交互式核磁共振（NMR）和计算机模拟研究确定了环A的两种模型化合物和环B的一种衍生物的构象。高分辨率NMR技术提供了结构信息，该信息通过分子动力学模拟得到进一步完善。这些方法正应用于该分子其余的受限片段。此构象信息将用于一种逐步构建法来确定整个分子的结构。
