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本文对A1修饰色氨酸胰岛素进行了晶体学的深入研究。晶体的空间群为R3,晶胞参数:a_H=80.3,c_H=37.5。应用立体化学制约最小二乘法并结合差值Fourier图人工分析对2.1的结构模型进行了多次调整和精化,最终偏离因子R=O.195。独立区两个A1-(L-色氨酸)胰岛素分子A链N端的A1色氨酸残基在电子密度图上表现十分清晰,其中分子ⅠA1色氨酸残基侧链具有两种构象。本文从结构角度推断三方四锌胰岛素分子Ⅱ的结构是一种低活性构象存在于六聚体内。此外,对有关胰岛素结构与功能的一些问题进行了讨论。
In this paper, A1 modified tryptophan insulin crystallography in-depth study. Crystal space group R3, unit cell parameters: a_H = 80.3, c_H = 37.5. Applying the three-dimensional chemical control least-square method combined with the Fourier analysis of difference figure, the structural model of 2.1 was adjusted and refined several times, with the final deviation factor of R = O.195. The A1 tryptophan residue at the N-terminus of the A chain of two A1- (L-tryptophan) insulin molecules in the independent region is clearly shown on the electron density map, in which the side chain of the molecule IA1 tryptophan has two conformations. In this paper, we deduced from the structural point of view the structure of the trigeminal zinc tetrazolium II molecule is a low activity conformation in hexamers. In addition, some questions about the structure and function of insulin are discussed.