Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter Campus 5, A-1030 Vienna, Austria.
Structure. 2010 Mar 14;18(4):416-9. doi: 10.1016/j.str.2010.03.003.
In this issue, Mittag et al. (2010) provided interesting insights concerning the molecular details of how the meandering of disordered proteins in conformational space can lead to collective binding modes and ultrasensitive probing of cellular kinase activities.
在本期中，Mittag 等人（2010 年）提供了有关无序蛋白质在构象空间中蜿蜒曲折如何导致集体结合模式和对细胞激酶活性进行超灵敏探测的分子细节的有趣见解。
