Aggregated amyloid β-peptide (Aβ) in small oligomeric forms inside the brain causes
synaptic function disruption and the development of Alzheimer's disease (AD). Histidine is …

Although various higher-order protein structure prediction methods have been developed,
almost all of them were developed based on the three-dimensional (3D) structure …

The l-α-Asp residues in peptides or proteins are prone to undergo nonenzymatic reactions to
form l-β-Asp, d-α-Asp, and d-β-Asp residues via a succinimide five-membered ring …

Molecular dynamics simulations of amyloid β1–42 containing d-aspartic acid residues were
performed using several continuous solvent models to investigate the usefulness of …

Recently, non-enzymatic stereoinversions of aspartic acid (Asp) residues in proteins and
peptides have been reported. Here, we performed replica exchange molecular dynamics …

Recently, stereoinversions and isomerizations of amino acid residues in the proteins of
living beings have been observed. Because isomerized amino acids cause structural …

In order to elucidate the reason why glutamic acid residues have lesser racemisation
reactivity than asparaginic acid, we investigated the racemisation energy barrier of …

In contrast with the common belief that all the amino acid residues in higher organisms are l‐
forms, d‐amino acid residues have been recently detected in various aging tissues. Aspartic …

The growing interest for peptide therapeutics calls for new strategies to determine the
physico-chemical properties responsible for the interactions of peptides with the …

Aspartic acid (Asp) residues are prone to non-enzymatic stereoinversion, and Asp-residue
stereoinversion is believed to be mediated via a succinimide (SI) intermediate. The …