title: Automatic assignment of the intrinsically disordered protein Tau with 441-residues.
abstract: 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.
authors.affiliation: Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen, Germany.
authors.forename: Rhagavendran L
authors.initials: RL
authors.lastname: Narayanan
authors.forename: Ulrich H N
authors.initials: UH
authors.lastname: Dürr
authors.forename: Stefan
authors.initials: S
authors.lastname: Bibow
authors.forename: Jacek
authors.initials: J
authors.lastname: Biernat
authors.forename: Eckhard
authors.initials: E
authors.lastname: Mandelkow
authors.forename: Markus
authors.initials: M
authors.lastname: Zweckstetter
mesh_terms: D000595:Amino Acid Sequence; D019295:Computational Biology; D030562:Databases, Protein; D001330:Electronic Data Processing; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000592:standards; D011487:Protein Conformation; D020033:Protein Isoforms / Q000737:chemistry; D012015:Reference Standards; D016875:tau Proteins / Q000737:chemistry*
chemical_list: D020033:Protein Isoforms; D016875:tau Proteins