AbstractWe explore the relative contributions of different structural elements to the stability of Aβ fibrils by molecular-dynamics simulations performed over a broad range of temperatures (298K to 398K). Our fibril structures are based on solid-state nuclear magnetic resonance experiments of Aβ(1–40) peptides, with sheets of parallel β-strands connected by loops and stabilized by interior salt bridges. We consider models with different interpeptide interfaces, and different staggering of the N- and C-terminal β-strands along the fibril axis. Multiple 10–20ns molecular-dynamics simulations show that fibril segments with 12 peptides are stable at ambient temperature. The different models converge toward an interdigitated side-chain packing, ...
AbstractWe investigate Aβ17-42 protofibril structures in solution using molecular dynamics simulatio...
AbstractThe free energy landscape for folding of the Alzheimer’s amyloid-β(25–35) peptide is explore...
Secondary nucleation pathways in which existing amyloid fibrils catalyze the formation of new aggreg...
AbstractWe explore the relative contributions of different structural elements to the stability of A...
We explore the relative contributions of different structural elements to the stability of Abeta fib...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We investigate Aβ17-42 protofibril structures in solution using molecular dynamics simulations. Rece...
AbstractUsing all-atom molecular dynamics, we study the temperature-induced dissociation of Aβ monom...
AbstractReplica exchange molecular dynamics and an all-atom implicit solvent model are used to probe...
A key player in Alzheimer’s disease is the peptide amyloid-beta (Aβ), whose aggregation into small s...
AbstractWe investigate Aβ17-42 protofibril structures in solution using molecular dynamics simulatio...
AbstractThe free energy landscape for folding of the Alzheimer’s amyloid-β(25–35) peptide is explore...
Secondary nucleation pathways in which existing amyloid fibrils catalyze the formation of new aggreg...
AbstractWe explore the relative contributions of different structural elements to the stability of A...
We explore the relative contributions of different structural elements to the stability of Abeta fib...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We present a simulation study of the early events of peptide dissociation from a fibril of the Alzhe...
We investigate Aβ17-42 protofibril structures in solution using molecular dynamics simulations. Rece...
AbstractUsing all-atom molecular dynamics, we study the temperature-induced dissociation of Aβ monom...
AbstractReplica exchange molecular dynamics and an all-atom implicit solvent model are used to probe...
A key player in Alzheimer’s disease is the peptide amyloid-beta (Aβ), whose aggregation into small s...
AbstractWe investigate Aβ17-42 protofibril structures in solution using molecular dynamics simulatio...
AbstractThe free energy landscape for folding of the Alzheimer’s amyloid-β(25–35) peptide is explore...
Secondary nucleation pathways in which existing amyloid fibrils catalyze the formation of new aggreg...