Differential scanning calorimetry studies of NaCl effect on the inverse temperature transition of some elastin-based polytetra-, polypenta-, and polynonapeptides (original) (raw)

This study investigates the effect of sodium chloride (NaCl) on the inverse temperature transition of elastin-based polypeptides, specifically polytetra-, polypenta-, and polynonapeptides, utilizing differential scanning calorimetry (DSC). The research highlights how the presence of NaCl influences the hydrophobic interactions within these polypeptides, modulating their structural characteristics and cloud point behavior. The findings provide valuable insights into the solvent effects on protein folding and the mechanistic underpinnings of the phase transition in elastin-like peptides.