Original Article
Structural character of ÃÂ
Abstract
The dynamics and structural character of ï¡-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 ï¡-syn12 peptide adopts in water an ï¡-helix structure at high pH. These results are distinct from other amyloid disease protein at neutral pH.