Automatic Assignment of the Intrinsically Disordered Protein Tau with 441-Residues

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• 作者：Rhagavendran L. Narayanan ; Ulrich H. N. Drr ; Stefan Bibow ; Jacek Biernat ; Eckhard Mandelkow ; Markus Zweckstetter
• 刊名：Journal of the American Chemical Society
• 出版年：2010
• 出版时间：September 1, 2010
• 年：2010
• 卷：132
• 期：34
• 页码：11906-11907
• 全文大小：153K
• 年卷期：v.132,no.34(September 1, 2010)
• ISSN：1520-5126

文摘

Intrinsically disordered proteins carry out many important functions in the cell. However, the lack of an ordered structure causes dramatic signal overlap and complicates the NMR-based characterization of their structure and dynamics. Here we demonstrate that the resonance assignment of 441-residue Tau and its smaller isoforms, htau24 (383 residues) and htau23 (352 residues), three prototypes of intrinsically disordered proteins, which bind to microtubules and play a key role in Alzheimer disease, can be obtained within 5 days by a combination of seven-dimensional NMR spectra with optimized methods for automatic assignment. Chemical shift differences between the three isoforms provide evidence for the global folding of Tau in solution.