Polymerization of the amyloid β-peptide (Aβ), a process which requires that the helical
structure of Aβ unfolds beforehand, is suspected to cause neurodegeneration in Alzheimer's …

Using replica exchange molecular dynamics, we study the effect of Asp23Tyr mutation on
Aβ10− 40 fibril growth. The effect of this mutation is revealed through the computation of free …

To study the early stage of amyloid‐β peptide (Aβ) aggregation, hexamers of the wild‐type
(WT) Aβ16–35 and its mutants with amyloid‐like conformations have been studied by …

Aggregation of the full‐length amyloid‐β (Aβ) and β2‐microglobulin (β2m) proteins is
associated with Alzheimer's disease and dialysis‐related amyloidosis, respectively. This …

It is experimentally known that oligomerization of amyloid beta peptides is accompanied by
a conformational transition from mainly alpha or random coil to beta sheets. The aim of this …

It is known that oligomers of amyloid-β (Aβ) peptide are associated with Alzheimer's disease.
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …

Amyloid formation is associated with many neurodegenerative diseases. Recent findings
suggest that early oligomeric aggregates could be major sources of toxicity. We present a …

The b‐hairpin is a building block in the β‐sheet structure. Understanding the formation of the
β‐hairpin may provide insight into the formation of β‐sheet structures in, for example, protein …

Most proteins do not aggregate while in their native functional states. However, they may be
disturbed from their native conformation by certain change in the environment, and form …

Peptide misfolding and aggregation are the early steps during the formation of amyloid
fibrils. Understanding these processes in detail is crucial for the development of therapeutic …