We describe here experiments designed to characterize the secondary structure of amyloid
fibrils of the Alzheimer's amyloid plaque peptide Aβ, using hydrogen-deuterium exchange …

We report here structural differences between Aβ (1-40) protofibrils and mature amyloid
fibrils associated with Alzheimer's disease as determined using hydrogen-deuterium …

Protofibrils are transient structures observed during in vitro formation of mature amyloid
fibrils and have been implicated as the toxic species responsible for cell dysfunction and …

We describe here details of the hydrogen− deuterium (H/D) exchange behavior of the
Alzheimer's peptide Aβ1-40, while it is a resident in the amyloid fibril, as determined by high …

The elucidation of the structure of amyloid fibrils and related aggregates is an important step
toward understanding the pathogenesis of diseases like Alzheimer's disease, which feature …

We describe methods for minimization of and correction for artifactual forward and backward
exchange occurring during hydrogen exchange–mass spectrometric (HX–MS) studies of …

The aggregation of proteins into amyloid fibrils is a complex and fascinating process
associated with debilitating clinical disorders such as Alzheimer's and Parkinson's diseases …

Although the amyloid fibrils formed from the Alzheimer's disease amyloid peptide Aβ are rich
in cross-β sheet, the peptide likely also exhibits turn and unstructured regions when it …

Alzheimer disease is a neurodegenerative disorder that is tightly linked to the self-assembly
and amyloid formation of the 39–43-residue-long amyloid-β (Aβ) peptide. Considerable …

β-Amyloid peptide (Aβ) is the primary protein component of senile plaques in Alzheimer's
disease and is believed to be responsible for the neurodegeneration associated with the …