We studied comprehensively the helicity and H-bonding evolutions during the folding processes of Lysand Arg-containing alanine-based peptides. The evolution of a-helical conformation concerning the entire sequence and each amino acid residue was examined, as well as the helix-forming propensities were characterized. The formation of various types of the intramolecular H-bonds was also investigated, pointing out the helix-stabilizing role of local interactions and the destabilizing role of non-local interplays. Our study led to the observation that the nonlocal H-bonds affected the evolution of helical conformations, as well as the entire folding processes.
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