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

ABSTRACT: 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, whereas 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, small angle x-ray scattering measurements were performed in native buffer in the absence of denaturant for a designed point mutant of the C-terminal domain of L9, a small cooperatively folded α-β protein, at 14 different temperatures over the range of 5-60°C. The I98A mutation destabilizes the domain such that both the DSE and the folded state are populated at 25°C in the absence of denaturant or

SUBMITTER: Stenzoski NE 

PROVIDER: S-EPMC6104559 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature