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Automatic assignment of the intrinsically disordered protein Tau with 441-residues.

Authors
  • Narayanan, Rhagavendran L
  • Dürr, Ulrich H N
  • Bibow, Stefan
  • Biernat, Jacek
  • Mandelkow, Eckhard
  • Zweckstetter, Markus
Type
Published Article
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society
Publication Date
Sep 01, 2010
Volume
132
Issue
34
Pages
11906–11907
Identifiers
DOI: 10.1021/ja105657f
PMID: 20687558
Source
Medline
License
Unknown

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.

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