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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Abstract
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 |
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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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