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 …

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 …

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 …

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

AD (Alzheimer's disease) is a neurodegenerative disorder characterized by self-assembly
and amyloid formation of the 39–43 residue long Aβ (amyloid-β)-peptide. The most …

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

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 …

A general method to analyze the structure of a supramolecular complex of amyloid fibrils at
amino acid residue resolution has been developed. This method combines the NMR …

We report investigations of the molecular structure of amyloid fibrils formed by residues 14–
23 of the β-amyloid peptide associated with Alzheimer's disease (Aβ 14-23), using solid …

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 …