Nishikawa Ken
Department of Bioinformatics, Maebashi Institute of Technology, 460-1 Kamisadori, Maebashi, Gunma 371-0816, Japan.
Biophysics (Nagoya-shi). 2009 Oct 21;5:53-58. doi: 10.2142/biophysics.5.53. eCollection 2009.
Proteins with wholly or partly denatured structures are called intrinsically disordered or natively unfolded proteins (NUPs). Functional importance of NUPs was revealed by NMR studies as first reviewed by P. Wright in 1999. Since then, computational analyses on NUPs have also been intensively carried out to predict that approximately one third of eukaryotic proteins are NUPs. I will start this overview with the question why it took so long to identify NUPs as an important subject of protein science, and then move on to several issues such as, whether or not NUPs are specific to eukaryotes, what a particularly higher fraction of NUPs existing in the nucleus means, and what evolutionary implications NUPs have.
具有完全或部分变性结构的蛋白质被称为内在无序或天然未折叠蛋白质（NUPs）。1999年P. Wright首次综述的核磁共振研究揭示了NUPs的功能重要性。从那时起，也对NUPs进行了深入的计算分析，以预测大约三分之一的真核生物蛋白质是NUPs。我将从为什么花了这么长时间才将NUPs确定为蛋白质科学的一个重要主题这个问题开始本综述，然后转向几个问题，例如，NUPs是否是真核生物特有的，细胞核中存在的NUPs比例特别高意味着什么，以及NUPs有什么进化意义。
