pH dependent thermodynamic and amide exchange studies of the C-terminal domain of the ribosomal protein L9: Implications for unfolded state structure

Amide H/D exchange studies and thermodynamic measurements are combined to probe pH dependent structure in the unfolded state of the small, mixed alpha-beta protein (C-terminal domain of the ribosomal protein L9) CTL9. The studies revealed that unfolded state of CTL9 contains significant interactions and are hydrophobic in nature that lead to compaction but are not sufficient to confer significant protection to hydrogen bonds.