What are the two mechanisms by which guanidine hydrochloride and urea denature proteins?

Guanidine hydrochloride and urea denature proteins involve two mechanisms:

The first mechanism is that the denatured protein binds preferentially to myochloride and urea to form a complex, when the complex is removed, the reaction equilibrium shifts, and as the concentration of the denaturant increases, the protein in its native state is continuously transformed into a complex, eventually resulting in a protein complete degeneration;

The second mechanism is the solubilization of hydrophobic amino acid residues by guanidine hydrochloride and urea. Because muscle hydrochloride and urea have the ability to form hydrogen bonds, guanidine hydrochloride and urea can break the hydrogen bond at high concentrations (4-8 mol/water solution). , As a result, muscle hydrochloride and urea become better solvents for non-polar residues, so that the hydrophobic residues inside the protein molecule can stretch and increase their solubility, so that the protein can be denatured to different degrees.