Diseases associated with protein fibril-formation, such as the prion diseases and
Alzheimer's disease, are gaining increased attention due to their medical importance and …

Molecular dynamics simulations in explicit water were carried out for two stacks, each
composed of six 10‐strand antiparallel β‐sheets for two peptides corresponding to the …

Abstract Beta-amyloid (1–42) is the most effective peptide in the formation of inter-synaptic
aggregate structures. These complex structures lead to disruption of the neural network and …

In this paper, all-atom molecular dynamics simulations in explicit solvent are used to
investigate the structural and dynamical determinants of the α-helical to β-hairpin …

Using all-atom explicit solvent model and exhaustive replica exchange molecular dynamics
simulations we studied the conformational ensembles of several amino-truncated Aβ …

Replica exchange molecular dynamics and all‐atom implicit solvent model are used to
compute the structural propensities in Aβ monomers, dimers, and Aβ peptides bound to the …

The 42‐amino acid Aβ, the major constituent of the senile plaque deposits of the brains of
Alzheimer's disease patients, exhibits a high degree of heterogeneity at its N‐terminus …

Structural properties of Aβ (16–35) fragment are investigated as a model for the amyloid-β
peptide excluding its coil-inducing terminals. Our replica-exchange molecular dynamics …

Aggregates of amyloid-β (Aβ) peptides are known to be related to Alzheimer's disease. Their
aggregation is enhanced at hydrophilic–hydrophobic interfaces, such as a cell membrane …

The major protein constituent of the deposits of Alzheimer's disease is the so‐called amyloid
β‐peptide (Aβ) which was derived from proteolysis of a large transmembrane amyloid …