Akhmedov N A, Makhmudova T A, Khalilov R I, Zeĭnalova N M
Bioorg Khim. 1995 Aug;21(8):587-9.
The spatial structure and conformations of rimorphin were investigated using theoretical conformational analysis. The spatial organization of the peptide can be described by a set of 11 low-energy conformations of the backbone. By solving the reverse conformational problem, a number of modified amino acid sequences ([Ala2], [Ala3], [MePhe9], [MeLys10], [MeVal11], and [MeVal12]-analogs of rimorphin) were determined that have spatial structures corresponding to the set of low-energy conformations and should, therefore, possess physiological activity.
使用理论构象分析研究了环吗啡肽的空间结构和构象。该肽的空间组织可以通过一组11种主链低能量构象来描述。通过解决反向构象问题，确定了许多修饰的氨基酸序列（环吗啡肽的[Ala2]、[Ala3]、[MePhe9]、[MeLys10]、[MeVal11]和[MeVal12]类似物），它们具有与低能量构象集相对应的空间结构，因此应该具有生理活性。
