Creighton T E
European Molecular Biology Laboratory, Meyerhofstrasse 1, 6900 Heidelberg, Germany.
Bioessays. 1992 Mar;14(3):195-9. doi: 10.1002/bies.950140310.
The best-characterized model pathway of protein folding, that of disulphide bond formation in the small protein BPTI, has been questioned recently. A reinvestigation of that pathway, using alternative methods, concluded that the intermediates with non-native disulphide bonds accumulated to lower levels than previously had been observed. On this basis, a revised pathway was proposed that simply omitted those intermediates. Even if totally correct, however, the new observations are not inconsistent with the important characteristics of the original pathway and even confirmed many of them. Certain crucial observations that were the experimental basis for the original pathway were ignored, and these observations invalidate the revised pathway.
蛋白质折叠领域中特征最明确的模型途径，即小蛋白BPTI中二硫键形成的途径，最近受到了质疑。利用其他方法对该途径进行的重新研究得出结论，具有非天然二硫键的中间体积累到的水平低于之前观察到的水平。在此基础上，提出了一条修订途径，该途径只是简单地省略了那些中间体。然而，即使新的观察结果完全正确，它们也与原始途径的重要特征并不矛盾，甚至还证实了其中许多特征。一些作为原始途径实验依据的关键观察结果被忽视了，而这些观察结果使修订后的途径无效。
