Havel T F, Wüthrich K
J Mol Biol. 1985 Mar 20;182(2):281-94. doi: 10.1016/0022-2836(85)90346-8.
An evaluation of the potential of nuclear magnetic resonance (n.m.r.) as a means of determining polypeptide conformation in solution is performed with the aid of a new distance geometry program which is capable of computing complete spatial structures for small proteins from n.m.r. data. Ten sets of geometric constraints which simulate the results available from n.m.r. experiments of varying precision and completeness were extracted from the crystal structure of the basic pancreatic trypsin inhibitor, and conformers consistent with these constraints were computed. Comparison of these computed structures with each other and with the original crystal structure shows that it is possible to determine the global conformation of a polypeptide chain from the distance constraints which are available from n.m.r. experiments. The results obtained with the different data sets also provide a standard by which the quality of protein structures computed from n.m.r. data can be evaluated when no crystal structure is available, and indicate directions in which n.m.r. experiments for protein structure determination could be further improved.
借助一个新的距离几何程序，对核磁共振（n.m.r.）作为确定溶液中多肽构象的一种手段的潜力进行了评估。该程序能够根据n.m.r.数据计算小蛋白质的完整空间结构。从碱性胰蛋白酶抑制剂的晶体结构中提取了十组几何约束条件，这些条件模拟了不同精度和完整性的n.m.r.实验可得的结果，并计算了与这些约束条件相符的构象。将这些计算得到的结构相互比较，并与原始晶体结构进行比较，结果表明，根据n.m.r.实验可得的距离约束条件能够确定多肽链的整体构象。当没有晶体结构可用时，使用不同数据集获得的结果也提供了一个标准，据此可以评估根据n.m.r.数据计算得到的蛋白质结构的质量，并指明了可进一步改进用于蛋白质结构测定的n.m.r.实验的方向。
