Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.
Journal of Biological ChemistryPublished 1 September 1994Open access
O. Schweers, E. Schönbrunn, Alexander Marx, Eckhard Mandelkow�
Citations558
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR
It is 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), because the protein is highly extended and the scattering is best described by that of a random ("Gaussian") polymer.
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).
Keywords
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