Abstract
We studied comprehensively the helicity and H-bonding evolutions during the folding processes of Lys- and Arg-containing alanine-based peptides. The evolution of α-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 non-local H-bonds affected the evolution of helical conformations, as well as the entire folding processes.
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Acknowledgments
This research was supported by the Hungarian Scientific Research Fund (OTKA PD 78554), and by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences (B. Leitgeb), and by TÁMOP-4.2.1/B-09/1/KONV-2010-0005.
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Leitgeb, B., Janzsó, G., Hudoba, L. et al. Helix and H-bond formations of alanine-based peptides containing basic amino acids. Struct Chem 22, 1287–1295 (2011). https://doi.org/10.1007/s11224-011-9824-x
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DOI: https://doi.org/10.1007/s11224-011-9824-x