Premium
Folding‐Unfolding Dynamics of pH‐Assisted Structures of S‐Peptide
Author(s) -
Perumalla D. Sravanakumar,
Govind Gokul,
Anjukandi Padmesh
Publication year - 2020
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.202000360
Subject(s) - peptide , protonation , chemistry , folding (dsp implementation) , rnase p , protein folding , biophysics , molecular dynamics , crystallography , ribonuclease , folding funnel , stereochemistry , computational chemistry , biochemistry , phi value analysis , rna , downhill folding , organic chemistry , biology , ion , electrical engineering , gene , engineering
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.