Akhmedov N A, Agaeva G A, Popov E M
Mol Biol (Mosk). 1987 Jan-Feb;21(1):174-81.
Spatial structure of peptide hormone secretin was investigated by the theoretical conformational method. A solution of the "direct conformational problem" for this hormone indicated that the possible structure of the secretin molecule under polar conditions may be described only by two families of low-energy conformations, possessing relatively conformational valid (Thr7-Leu22) and variable (His1-Phe6 and Leu23-Val27NH2) fragments. One of these families is comprised by five twists of the alpha-helix, while the second isoenergetic family possesses two short segments of the alpha-helix, divided by an irregular structure of the tetrapeptide.
采用理论构象方法研究了肽类激素促胰液素的空间结构。针对该激素的“直接构象问题”的解决方案表明，在极性条件下促胰液素分子的可能结构只能由两个低能量构象家族来描述，它们具有相对构象有效的片段（Thr7-Leu22）和可变片段（His1-Phe6和Leu23-Val27NH2）。其中一个家族由α-螺旋的五个扭曲组成，而第二个等能量家族具有两个α-螺旋短片段，被一个四肽的不规则结构隔开。
