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Folding-Unfolding Dynamics of pH-Assisted Structures of S-Peptide

Perumalla, DS and Govind, G and Anjukandi, P (2020) Folding-Unfolding Dynamics of pH-Assisted Structures of S-Peptide. In: ChemistrySelect, 5 (19). pp. 5748-5755.

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Official URL: https://doi.org/10.1002/slct.202000360


The folded form of S-Peptide is found to be essential for the activation of RNase-S complex. Herein the folding-unfolding dynamics of S-Peptide and its protonated form in mild acidic conditions are investigated to assess the most favorable folding pathway in physiological conditions. Our results confirm that the pH assisted S-peptide structures could indeed influence on the binding and collapse of the hydrophobic groups, which in turn can modulate the structural stability of S-Peptide α-helix. We affirm that the protonated S-Peptide has its partially and completely folded states which are readily accessible whereas in the case of non-protonated S-Peptide, there exists an energy barrier in attaining the folds. Further, the RNase-S complex formation could be mostly assisted by mild acidic pH and we also confirm that the folding-unfolding pathways of S-Peptide are independent of the pH. © 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim

Item Type: Journal Article
Publication: ChemistrySelect
Publisher: Wiley-Blackwell
Additional Information: The copyright of this article belongs to Wiley-Blackwell
Department/Centre: Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited: 05 Aug 2021 10:37
Last Modified: 05 Aug 2021 10:37
URI: http://eprints.iisc.ac.in/id/eprint/65593

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