Ontology highlight
ABSTRACT:
SUBMITTER: Mancini O
PROVIDER: S-EPMC6643746 | biostudies-literature | 2018 Nov
REPOSITORIES: biostudies-literature
Mancini Onorio O Rolinski Olaf J OJ Kubiak-Ossowska Karina K Mulheran Paul A PA
ACS omega 20181127 11
During the early stages of β amyloid (Ab) peptide aggregation, toxic oligomers form which have been recognized as a likely cause of Alzheimer's disease. In this work, we use fully atomistic molecular dynamics simulation to study the amorphous aggregation of the peptide as well as model β-sheet protofibril structures. In particular, we study the rotamer states of the single fluorescent tyrosine (Tyr) residue present in each Ab. We find that the occupation of the four previously identified rotamer ...[more]