Automatic assignment of the intrinsically disordered protein Tau with 441-residues.
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.
Narayanan
Rhagavendran L
RL
Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen, Germany.
Dürr
Ulrich H N
UH
Bibow
Stefan
S
Biernat
Jacek
J
Mandelkow
Eckhard
E
Zweckstetter
Markus
M
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*
D020033:Protein Isoforms; D016875:tau Proteins