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Molecular dynamics simulations method was used to study the dynamics and structural character of α-syn12 peptide complex with synphilin-1 protein in aqueous solution at low pH by using GROMOS 43A1 force field. The α-syn12 peptide aggregates faster at low pH than at neutral pH.
The structural and dynamics character of H1 peptide in aqueous solution has been investigated through temperature replica exchange molecular dynamics simulations with using two different water combined with OPLS-AA force field.
We have performed temperature replica exchange molecular dynamics simulations on α-syn12 peptide in aqueous solution by using GROMOS 43A1 force field. The dynamics and structural character under four different temperatures have been investigated through the backbone dihedral angle, representative structure etc.
The dynamics and structural character of α-syn12 peptide complex with synphilin-1 protein in aqueous solution has been investigated through molecular dynamics simulations by using GROMOS 43A1 force field. The structural character of α-syn12 peptide complex with synphilin-1 protein adopts in water a loop structure.
The dynamics and structural character of a-syn12 peptide in aqueous solution at high pH has been investigated through temperature replica exchange molecular dynamics simulations by using GROMOS 43A1 force field. The isolated a-syn12 peptide adopts in water an a-helix structure at high pH. These results are distinct from other amyloid disease protein at neutral pH.
The dynamics character of HI peptide in aqueous solution has been investigated through temperature replica exchange molecular dynamics simulations with using two different force fields (OPLS-AA and GROMOS). The simulation using OPLS-AA force field produced more sampling in the alpha region relative to GROMOS 43A1 force field.
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