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 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 …

Aβ peptides can assemble into amyloid fibrils, which represent one of the hallmarks of
Alzheimer's disease. Recent studies, however, have focused on the behavior of small …

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 …

Recent experimental evidence points to intermediates populated during the process of
amyloid fibril formation as the toxic moieties primarily responsible for the development of …

Metastable oligomeric and protofibrillar forms of amyloidogenic proteins have been
implicated as on-pathway assembly intermediates in amyloid formation and as the major …

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 …

Protein− protein interactions are frequently mediated by stable, intermolecular β-sheets. A
number of cytokines and the HIV Protease, for example, dimerize through β-sheet motifs …

Low pH has a strong stabilising effect on the fibrillar assembly of amyloid β, which is
associated with Alzheimer's disease. The stabilising effect is already pronounced at pH 6.0 …