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• W4293282502 endingPage "7" @default.
• W4293282502 startingPage "1" @default.
• W4293282502 abstract "The amyloid-beta peptide is a peptide that consists of 42 amino acids and is derived from the precursor protein known as an amyloid-beta precursor protein (APP). The amyloid-beta precursor protein is a glycoprotein that is a single-pass transmembrane transporter that only crosses the membrane once. On chromosome 21, you will find the gene that codes for amyloid-beta precursor protein. Because of its significance in biological applications, the protein's thermal characteristics is being investigated. The thermal behavior of this biostructure may be predicted using computer models, which are dependent on the structure's arrangement of atoms. Numerical molecular dynamics techniques (the Green-Kubo approach), the thermal behavior of amyloid beta-peptide is computed in the present computational work. In this approach, amyloid beta-peptide is formed by the atoms C, F, H, N, O, and S using the DREIDING and Universal force field (UFF). According to the findings of our MD simulations, the amyloid-beta protein has a thermal conductivity (k) of 1.23 W/mK under typical conditions ( T = 300 K and P = 1 bar). Simulations have also shown that the starting temperature and pressure significantly impact how the modeled protein reacts to heat. After t = 10 ns, thermal behavior is seen in the simulated structures, brought about by a rise in the starting temperature and pressure." @default.
• W4293282502 created "2022-08-27" @default.
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• W4293282502 date "2022-11-01" @default.
• W4293282502 modified "2023-09-30" @default.
• W4293282502 title "A molecular dynamic approach to a hypothesis on the dynamical behavior of Rosuvastatin on Alzheimer's disease amyloid beta-peptide interactions in the atomic structures" @default.
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• W4293282502 doi "https://doi.org/10.1016/j.enganabound.2022.08.010" @default.
• W4293282502 hasPublicationYear "2022" @default.
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