Automatic Assignment of the Intrinsically Disordered Protein Tau with 441-Residues
| Autor: | Rhagavendran L. Narayanan, Markus Zweckstetter, Ulrich H.N. Dürr, Eckhard Mandelkow, Stefan Bibow, Jacek Biernat |
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| Rok vydání: | 2010 |
| Předmět: |
Gene isoform
Magnetic Resonance Spectroscopy Protein Conformation Tau protein tau Proteins Intrinsically disordered proteins Biochemistry Catalysis Colloid and Surface Chemistry Protein structure Microtubule Humans Protein Isoforms Amino Acid Sequence Databases Protein Peptide sequence Electronic Data Processing biology Chemistry Computational Biology General Chemistry Reference Standards Folding (chemistry) NMR spectra database Crystallography Biophysics biology.protein |
| Zdroj: | Journal of the American Chemical Society |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja105657f |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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