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- W2010511290 abstract "The assembly dynamics of two β sheets with different initial separation distances are explored by multiple all-atom molecular dynamics simulations with the presence of explicit water solvent. The β sheet is composed of seven identical peptides in an antiparallel fashion. The peptide sequence is the 20–29 segment of human Islet amyloid polypeptide. Our simulations show that the assembly occurs not only in the lateral direction but also along the longitudinal direction, which provides a new insight into the assembly pathway at the early stage of fibril elongation. Based on Poisson–Boltzmann free energy analysis and quasiharmonic configuration entropy estimation, the entropic contribution is found to play an important role in the longitudinal assembly. Moreover, a possible oligomeric state with cyclic form is suggested based on one assembly model found in the simulations, illustrating the polymorphic nature of aggregation of the amyloidogenic peptide." @default.
- W2010511290 created "2016-06-24" @default.
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- W2010511290 date "2009-04-28" @default.
- W2010511290 modified "2023-09-23" @default.
- W2010511290 title "Assembly dynamics of two-β sheets revealed by molecular dynamics simulations" @default.
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- W2010511290 doi "https://doi.org/10.1063/1.3123532" @default.
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