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本文描述了单体胰岛素类似物去五肽(B26—B30)胰岛素的结构。同三方二锌胰岛素结构的详细比较说明,DPI虽然在结构上有一些大的改变,但是基本的二级结构单位仍然完整地保持着。像胰岛素的其他晶形那样,DPI结构比较接近于二锌胰岛素结构中的分子Ⅰ。除了结构表面的改变之外,在分子中心还有一些微妙和广泛的改变。分子在晶体中紧密地堆积,有着许多不同的接触,包括蛋白质-镉相互作用的复合网及大量以水为媒介的接触。分子表面大批疏水基团绕蛋白质群集而成一厚带。晶体结构具有良好的有序性,某些侧链的清晰度和水分子的确定性优于在更具活动性的三方二锌胰岛素六体晶体所得的结果。
Described herein are the structures of monomeric insulin analog depentopeptides (B26-B30) insulin. A detailed comparison of the structure of the two zinc insulin with the three parties shows that although there are some major structural changes in the DPI, the basic secondary structure units are still intact. Like other crystals of insulin, the DPI structure is closer to the molecule I in the zinc-insulin structure. In addition to the structural surface changes, there are some subtle and broad changes in the molecular center. Molecules are densely packed in crystals and have many different contacts, including a complex network of protein-cadmium interactions and a host of water-mediated contacts. A large number of hydrophobic molecules on the surface of the protein cluster formed a thick belt. The crystal structure is well ordered, the clarity of some side chains and the certainty of water molecules outweigh the results obtained with the more active trisodium zinc hexagonal crystals.