This suggests that there may be significant structural differences between Aβ M01–42 fibrils and Aβ M01–40 fibrils, which may be a result of their different hydrophobicities and steric constraints related to accommodating two extra residues within the fibril. 71 Furthermore, we note that the location of the β-strands in this work are in slightly different locations compared to many of those reported for Aβ 1–40 fibrils.
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High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.
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