Testa Lorenzo, Brocca Stefania, Santambrogio Carlo, D'Urzo Annalisa, Habchi Johnny, Longhi Sonia, Uversky Vladimir N, Grandori Rita
Department of Biotechnology and Biosciences; University of Milano-Bicocca; Milan, Italy.
Aix-Marseille Université; CNRS, Architecture et Fonction des Macromolécules Biologiques (AFMB); Marseille, France.
Intrinsically Disord Proteins. 2013 Apr 1;1(1):e25068. doi: 10.4161/idp.25068. eCollection 2013 Jan-Dec.
Intrinsically disordered proteins (IDPs) exert key biological functions but tend to escape identification and characterization due to their high structural dynamics and heterogeneity. The possibility to dissect conformational ensembles by electrospray-ionization mass spectrometry (ESI-MS) offers an attracting possibility to develop a signature for this class of proteins based on their peculiar ionization behavior. This review summarizes available data on charge-state distributions (CSDs) obtained for IDPs by non-denaturing ESI-MS, with reference to globular or chemically denatured proteins. The results illustrate the contributions that direct ESI-MS analysis can give to the identification of new putative IDPs and to their conformational investigation.
内在无序蛋白（IDP）发挥着关键的生物学功能，但由于其高度的结构动态性和异质性，往往难以被识别和表征。通过电喷雾电离质谱（ESI-MS）剖析构象集合的可能性为基于这类蛋白质独特的电离行为开发其特征标记提供了诱人的前景。本综述总结了通过非变性ESI-MS获得的IDP电荷态分布（CSD）的现有数据，并与球状或化学变性蛋白进行了对比。结果表明，直接的ESI-MS分析可为新的潜在IDP的识别及其构象研究做出贡献。
