Gadzhieva Sh N, Akhmedov N A, Masimov É A, Godzhaev N M
Biofizika. 2013 Jul-Aug;58(4):587-90.
The spatial structure of cardioactive Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 molecule has been investigated using a theoretical conformational analysis. The low-energy conformations of the molecule were found, the values of the backbone and side T-T chain dihedral angles of amino acid residues constituting the peptide were determined, and the energies of intra- and interresidual interactions were estimated. It is revealed that the spatial structure of this molecule can exist in 11 stable backbone forms.
已使用理论构象分析研究了具有心脏活性的苏氨酸 - 脯氨酸 - 丙氨酸 - 谷氨酸 - 天冬氨酸 - 苯丙氨酸 - 甲硫氨酸 - 精氨酸 - 苯丙氨酸 - 氨基分子的空间结构。发现了该分子的低能构象，确定了构成该肽的氨基酸残基的主链和侧链T - T链二面角的值，并估算了残基内和残基间相互作用的能量。结果表明，该分子的空间结构可以以11种稳定的主链形式存在。
