The Unfolded State of the C-Terminal Domain of L9 Expands at Low Temperature but not at Elevated Temperatures

The temperature dependence of the overall dimensions of the denatured state ensemble (DSE) of proteins remains unclear. Some studies indicate compaction of the DSE at high temperatures, while others argue that dimensions do not decrease. The degree of compaction or expansion in the cold denatured state has been less studied. To investigate the temperature dependence of unfolded state dimensions, SAXS measurements were performed in native buffer in the absence of denaturant for a designed point mutant of the C-terminal domain of L9 (CTL9), a small cooperatively folded α-β protein, at 14 different temperatures over the range of 5-60°C.

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