Folding Thermodynamics and Kinetics of the N-Terminal Domain of the Circadian Clock-Regulated Histidine Kinase SasA.
Folding behavior and timing of the clock-controlled enzyme SasA's front section
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Abstract
Proline isomerization is identified as a rate-limiting step in the folding of the N-terminal thioredoxin-like domain of histidine kinase SasA.
- The study focuses on the folding kinetics of the N-SasA domain, which is crucial for the cyanobacterial circadian clock.
- Thermodynamic stability of N-SasA was assessed under thermal and chemical denaturation conditions.
- Energy barriers for both folding and unfolding processes were determined.
- Intrinsic tryptophan fluorescence and nuclear magnetic resonance spectroscopy were utilized to analyze folding kinetics.
- Accelerated folding kinetics were observed when peptidyl-prolyl cis/trans isomerase was present.
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