Krüger P, Strassburger W, Wollmer A, van Gunsteren W F, Dodson G G
Eur Biophys J. 1987;14(8):449-59. doi: 10.1007/BF00293254.
Insulin crystallizes in different forms, some of which show different conformations for the different molecules in the asymmetric unit. This observation leads to the question as to which conformation the molecule will adopt in solution. Molecular dynamics computer simulations of rhombohedral 2 Zn pig insulin have been carried out for both monomers (1 and 2) independently in order to study their behaviour in the absence of quaternary structure and crystal packing forces. These preliminary 120 ps simulations suggest that both monomers converge in solution to very similar conformations which differ from the X-ray structures of both monomer 1 and 2 (Chinese nomenclature), but are closer to the former, as has previously been suggested by an analysis of the crystal packing (Chothia et al. 1983) and by energy minimization (Wodak et al. 1984). The secondary structure of the molecules is basically preserved, as expected. A detailed description of the conformational changes is given.
胰岛素以不同形式结晶，其中一些在不对称单元中的不同分子呈现出不同构象。这一观察结果引发了关于该分子在溶液中会采取何种构象的问题。为了研究菱形2锌猪胰岛素单体（1和2）在不存在四级结构和晶体堆积力的情况下的行为，分别对它们进行了分子动力学计算机模拟。这些初步的120皮秒模拟表明，两种单体在溶液中收敛到非常相似的构象，这与单体1和2（中国命名法）的X射线结构不同，但如先前通过晶体堆积分析（乔西亚等人，1983年）和能量最小化（沃达克等人，1984年）所表明的那样，更接近前者。正如预期的那样，分子的二级结构基本得以保留。文中给出了构象变化的详细描述。
