Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, PO Box 7, 1518 Budapest, Hungary.
J Mol Biol. 2010 Oct 29;403(3):346-50. doi: 10.1016/j.jmb.2010.07.044. Epub 2010 Sep 15.
Although intrinsically disordered proteins are prevalent and functionally important, it has never been asked whether structural disorder should be considered as a separate structural category on its own or merely as a lack of secondary and/or tertiary structure. We address this issue by showing that its length distribution in the human proteome follows a power law, with many short regions but also a significant incidence of very long disordered regions. This behavior is in sharp contrast with that of conventional secondary structural elements and is highly reminiscent of the distribution of tertiary structural units in proteins. We interpret this finding by the direct functional involvement of disorder, which distinguishes it from secondary structural elements and endows it with tertiary structural attributes.
尽管无规卷曲蛋白质普遍存在且具有重要的功能，但人们从未问过是否应将结构无序视为一个独立的结构类别，还是仅仅将其视为缺乏二级和/或三级结构。我们通过展示人类蛋白质组中其长度分布遵循幂律来解决这个问题，其中有许多短区域，但也有很长的无序区域。这种行为与传统的二级结构元件形成鲜明对比，非常类似于蛋白质中三级结构单元的分布。我们通过无序的直接功能参与来解释这一发现，这将其与二级结构元件区分开来，并赋予其三级结构属性。
