Flexibility and solvation of amyloid-β hydrophobic core
L Vugmeyster, MA Clark, IB Falconer… - Journal of Biological …, 2016 - ASBMB
Amyloid fibril deposits found in Alzheimer disease patients are composed of amyloid-β (Aβ)
protein forming a number of hydrophobic interfaces that are believed to be mostly rigid. We
have investigated the μs-ms time-scale dynamics of the intra-strand hydrophobic core and
interfaces of the fibrils composed of Aβ 1–40 protein. Using solid-state 2 H NMR line shape
experiments performed on selectively deuterated methyl groups, we probed the 3-fold
symmetric and 2-fold symmetric polymorphs of native Aβ as well as the protofibrils of D23N …
protein forming a number of hydrophobic interfaces that are believed to be mostly rigid. We
have investigated the μs-ms time-scale dynamics of the intra-strand hydrophobic core and
interfaces of the fibrils composed of Aβ 1–40 protein. Using solid-state 2 H NMR line shape
experiments performed on selectively deuterated methyl groups, we probed the 3-fold
symmetric and 2-fold symmetric polymorphs of native Aβ as well as the protofibrils of D23N …
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