van Gunsteren W F, Berendsen H J
J Mol Biol. 1984 Jul 15;176(4):559-64. doi: 10.1016/0022-2836(84)90177-3.
Knowledge about the architecture of macromolecules has been derived primarily from crystallography. Therefore, it has been a matter of concern whether the conformation of a macromolecule in solution, namely in vivo, might be different from that in the crystalline state. To determine the difference between the conformations, a protein (trypsin inhibitor) dissolved in water has been simulated using the method of molecular dynamics and the results are compared with those obtained from a simulation of the full crystalline unit cell. We report here that no significant difference was found for backbone atoms, except for two more or less flexible loops extending from the core of the protein and the very flexible carboxyterminal residues. The side-chains in which the conformation in solution differs considerably from that in the crystal all belong to polar residues.
关于大分子结构的知识主要来自晶体学。因此，一个大分子在溶液中（即在体内）的构象是否可能与晶体状态下的构象不同，一直是人们关注的问题。为了确定构象之间的差异，使用分子动力学方法对溶解在水中的一种蛋白质（胰蛋白酶抑制剂）进行了模拟，并将结果与从完整晶体晶胞模拟中获得的结果进行了比较。我们在此报告，除了从蛋白质核心延伸出的两个或多或少具有柔性的环和非常柔性的羧基末端残基外，主链原子未发现显著差异。溶液中构象与晶体中构象有很大不同的侧链均属于极性残基。
