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• W2002487446 abstract "In this study, molecular dynamics simulations were carried out on Lys- and Arg-containing Ala-based peptides (i.e. Ace-(AAAAK)(n)A-NH(2) and Ace-(AAAAR)(n)A-NH(2), where n=1-4), in order to explore and characterize their folding processes. For the oligopeptides, the evolution of α-helical structure with regard to the whole conformation, as well as to each residue was investigated, and the helix-forming propensities were characterized. On the basis of the helicity curves, representing the alteration of average helicity as a function of time, the typical time values describing the folding processes and subprocesses were identified. In the case of each peptide, the evolution and role of helix-stabilizing, non-local and side-chain-to-backbone H-bonds were examined. The appearing i←i+4 H-bonds pointed out the role of these interactions in the stabilization of α-helical conformations, while the occurring i←i+3 H-bonds indicated the presence of β-turn or 3(10)-helical structures. Studying the formation and role of non-local and side-chain-to-backbone H-bonds led to the observation that these types of interactions produced an effect on the evolution of helical conformations, as well as on the folding processes." @default.
• W2002487446 created "2016-06-24" @default.
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• W2002487446 date "2011-08-01" @default.
• W2002487446 modified "2023-10-17" @default.
• W2002487446 title "Exploring and characterizing the folding processes of Lys- and Arg-containing Ala-based peptides: A molecular dynamics study" @default.
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• W2002487446 doi "https://doi.org/10.1016/j.compbiolchem.2011.05.004" @default.
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