Murrali Maria Grazia, Schiavina Marco, Sainati Valerio, Bermel Wolfgang, Pierattelli Roberta, Felli Isabella C
CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.
Bruker BioSpin GmbH, Silberstreifen, 76287, Rheinstetten, Germany.
J Biomol NMR. 2018 Mar;70(3):167-175. doi: 10.1007/s10858-018-0167-4. Epub 2018 Feb 28.
The increasingly recognized biological relevance of intrinsically disordered proteins requires a continuous expansion of the tools for their characterization via NMR spectroscopy, the only technique so far able to provide atomic-resolution information on these highly mobile macromolecules. Here we present the implementation of projection spectroscopy in C-direct detected NMR experiments to achieve the sequence specific assignment of IDPs. The approach was used to obtain the complete backbone assignment at high temperature of α-synuclein, a paradigmatic intrinsically disordered protein.
内在无序蛋白质日益被认识到的生物学相关性,要求不断扩展通过核磁共振波谱对其进行表征的工具,核磁共振波谱是迄今为止唯一能够提供关于这些高度动态大分子的原子分辨率信息的技术。在此,我们展示了在碳直接检测核磁共振实验中投影光谱的应用,以实现内在无序蛋白质的序列特异性归属。该方法被用于在高温下获得α-突触核蛋白(一种典型的内在无序蛋白质)的完整主链归属。