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• W2316953060 abstract "The paper presents comparative data on the impact of force-fields AMBER (ff03, ff99SB, and ff96) on the results of molecular dynamics experiments with dimeric molecules formed by ion-peptide NH 2 -(RADA) 4 -COOH in the β-conformation at two temperatures (300K and 320K). It is shown that an MD simulation in explicit water environment is the most informative approach. The use of different force-fields has a significant influence on the stability of the initial molecular conformation of the peptide over time. Finally, the simulation in ff99SB environment provides significant stability of antiparallel β-structure of the dimer at 300K, while ff96 not only ensures the highest stability of the initial b-peptide conformation at higher temperatures, but also enhances the retention of antiparallel β-conformation, which determines the ability of NH 2 -(RADA) 4 -COOH peptides to self-organization." @default.
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• W2316953060 date "2011-03-04" @default.
• W2316953060 modified "2023-09-26" @default.
• W2316953060 title "On the choice of force fields for studying the molecular dynamics of ion peptides and their dimers" @default.
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• W2316953060 doi "https://doi.org/10.17537/2011.6.53" @default.
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