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Cited by 567

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Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.

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Schweers, O., Schönbrunn-Hanebeck, E., Marx, A., Mandelkow, E.·1994·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)51080-8
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Abstract

We have studied the conformation of tau protein and Alzheimer paired helical filaments (PHF) by several spectroscopic, scattering, and imaging methods revealing the overall shape and the conformation of the polypeptide backbone. Tau protein behaves in solution as if it were denatured; no evidence for compact folding was detected. The protein is highly extended, there is no defined radius of gyration, and the scattering is best described by that of a random ("Gaussian") polymer. CD and Fourier transform infrared spectroscopy show only a minimal content of ordered secondary structure (alpha-helix or beta-sheet). Similarly, PHFs from Alzheimer brain tissue show no detectable secondary structure by x-ray diffraction or spectroscopy. It is thus unlikely that the aggregation of tau into Alzheimer PHFs is based on interactions between strands of beta-sheets (a model currently favored for other disease-related polymers such as beta-amyloid fibers of Alzheimer's disease).

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Metadata

Authors
Schweers, O., Schönbrunn-Hanebeck, E., Marx, A., & Mandelkow, E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1994-09
Volume
269
Issue
39
Pages
24290-24297
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)51080-8
OpenAlex
W1525659758
Cited by
567
References
2
FWCI
5.98
Type
journal article
Language
en
Open access
hybrid
Licence

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CoChat. (2026). Citation check: Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. https://app.cochat.ai/papers/10.1016/s0021-9258(19)51080-8
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Schweers, O., Schönbrunn-Hanebeck, E., Marx, A., & Mandelkow, E. (1994). Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)51080-8

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