Crippen G M
Int J Pept Protein Res. 1979 Mar;13(3):320-6. doi: 10.1111/j.1399-3011.1979.tb01886.x.
Many physico-chemical studies are made on proteins to determine something of their solution conformation. For example the coat protein of Tobacco Mosaic Virus has been subjected to more non-crystallographic experimental studies to determine its native conformation than perhaps any other protein. Yet the sum of the experimentally determined constraints on its tertiary structure are surprisingly inadequate to fix its conformation. We are able to detect and remove minor inconsistencies in the data and then calculate a sampling of conformations consistent with all the data, which differ among themselves by r.m.s. deviations of the respective interresidue distances ranging from 5.7 angstrom to 15.8 angstrom. Some individual interresidue distances differ by as much as 50 angstrom from structure to structure. In order to restrict the range of possible conformations to something corresponding to the errors in a 10 angstrom resolution X-ray crystal structure, chemical and spectroscopic studies will have to be much more detailed than anything done to date. Our calculations appear to be useful in deciding which further experiments would be most productive.
人们对蛋白质进行了许多物理化学研究，以确定其溶液构象的某些情况。例如，烟草花叶病毒的外壳蛋白接受的非晶体学实验研究比其他任何蛋白质都要多，目的是确定其天然构象。然而，通过实验确定的对其三级结构的限制条件之和，竟然不足以确定其构象。我们能够检测并消除数据中的微小不一致性，然后计算出与所有数据一致的构象样本，这些构象之间各自残基间距离的均方根偏差在5.7埃至15.8埃之间。不同结构之间，一些个别残基间距离相差多达50埃。为了将可能的构象范围限制在与10埃分辨率的X射线晶体结构误差相对应的范围内，化学和光谱研究必须比迄今为止所做的任何研究都要详细得多。我们的计算结果似乎有助于确定哪些进一步的实验将最有成效。
