Ultra-high field NMR studies of antibody binding and site-specific phosphorylation of α-synuclein
Ultra-high field NMR studies of antibody binding and site-specific phosphorylation of α-synuclein
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DOI：
10.1016/j.bbrc.2007.09.048
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发表时间：
2007-11-23
影响因子：
3.1
通讯作者：
Kato, Koichi
中科院分区：
文献类型：
--
作者：
Sasakawa, Hiroaki;Sakata, Eri;Kato, Koichi
尽管人们逐渐认识到本质上无序蛋白质的生物学重要性，但由于化学位移分散性差，这类蛋白质的 NMR 分析仍然是更具挑战性的任务。预计超高场核磁共振波谱可以提供更高的分辨率来应对这一困难。在这里，我们报告了对α-突触核蛋白的超高场核磁共振研究，α-突触核蛋白是一种本质上无序的蛋白质，被确定为路易体的主要成分。基于在 920 MHz 质子频率收集的 NMR 光谱数据，我们进行了抗 α-突触核蛋白单克隆抗体的表位作图，此外，还表征了 α-突触核蛋白 Ser129 磷酸化的构象效应。 (C) 2007 Elsevier Inc. 保留所有权利。
Although biological importance of intrinsically disordered proteins is becoming recognized, NMR analyses of this class of proteins remain as tasks with more challenge because of poor chemical shift dispersion. It is expected that ultra-high field NMR spectroscopy offers improved resolution to cope with this difficulty. Here, we report an ultra-high field NMR study of alpha-synuclein, an intrinsically disordered protein identified as the major component of the Lewy bodies. Based on NMR spectral data collected at a 920 MHz proton frequency, we performed epitope mapping of an anti-alpha-synuclein monoclonal antibody, and furthermore, characterized conformational effects of phosphorylation at Serl29 of ot-synuclein. (C) 2007 Elsevier Inc. All rights reserved.