Effect of Cosolutes on Lysozyme

Using solution X-ray scattering we investigated the folding equilibrium of egg-white lysozyme in the presence of the denaturating cosolutes urea and GuHCl. We showed that urea causes lysozyme to gradually assume a structure with molten globule characteristics, while GuHCl causes lysozyme to assume a random coil structure. In both cases, equilibrium intermediate states were hardly detected (ACS Omega 2018).

Lyz
The unfolding of lysozyme increases with increasing the concentration of the weakly denaturating cosolutes urea and GuHCl.