What is the most likely mode of protein denaturation by urea, based on its structure?

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Questions are based on the following passage: The homodimeric DNA-binding protein Ssh10b, from Sulfolobus shibattae, is conserved in the majority of currently sequenced thermophilic and hyperthermophilic archaeal genomes. Denaturation of Ssh10b by urea, a chaotropic agent, was tested at five different pH values (3, 5, 7, 9, and 10) and eight different NaCl salt concentrations (0 M [black squares], 0.01 M [open squares], 0.02 M [black circles], 0.05 M [open circles], 0.1 M [black triangles], 0.2 [open triangles], 0.5 M [inverted black triangles], and 1 M [inverted open triangles]). The... Show more

What is the most likely mode of protein denaturation by urea, based on its structure?