Exploring and characterizing the folding processes of Lys- and Arg-containing Ala-based peptides: A molecular dynamics study
In this study, molecular dynamics simulations were carried out on Lys- and Arg-containing Ala-based peptides (i.e. Ace-(AAAAK)nA-NH2 and Ace-(AAAAR)nA-NH2, where n=14), in order to explore and characterize their folding processes. For the oligopeptides, the evolution of ?-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 ?-helical conformations, while the occurring i?i+3 H-bonds indicated the presence of ?-turn or 310-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.
folding process ala-based peptide molecular dynamics helical structure intramolecular h-bond folding pathway