Ismailova L I, Akhmedov N A, Abbasly R M
Biofizika. 2008 Jan-Feb;53(1):14-21.
The spatial structure of two cardioactive isoleucine pentapeptides Glu-Phe-Leu-Arg-Ile-NH2 (I) and Pro-Phe-Tyr-Arg-Ile-NH2 (II) have been investigated using the theoretical conformational analysis. The low-energy conformations of these molecules were found, the values of dihedral angles of the backbone and side chains of the amino acid residues constituting these peptides were determined, and the energies of intra- and interresidual interactions were estimated. It was revealed that the spatial structure of molecule I can exist as five and that of molecule II as seven stable backbone forms.
利用理论构象分析研究了两种具有心脏活性的异亮氨酸五肽Glu-Phe-Leu-Arg-Ile-NH2（I）和Pro-Phe-Tyr-Arg-Ile-NH2（II）的空间结构。发现了这些分子的低能构象，确定了构成这些肽的氨基酸残基主链和侧链的二面角值，并估算了残基内和残基间相互作用的能量。结果表明，分子I的空间结构可以以五种稳定主链形式存在，分子II的空间结构可以以七种稳定主链形式存在。
