Thermal stability analyses of human PERIOD-2 C-terminal domain using dynamic light scattering and circular dichroism.

ABSTRACT: At the molecular level, the circadian clock is regulated by a time delayed transcriptional-translational feedback loop in which the core proteins interact with each other rhythmically to drive daily biological rhythms. The C-terminal domain of a key clock protein PER2 (PER2c) plays a critically important role in the loop, not only for its interaction with the binding partner CRY proteins but also for the CRY/PER complex's translocation from the cytosol to the nucleus. Previous circular dichroism (CD) spectroscopic studies have shown that mouse PER2c (mPER2c) is less structured in solution by itself but folded into stable secondary structures upon interaction with mouse CRYs. To understand the stability and folding of human PER2c (hPER2c), we expressed and purified hPER2c. Three oligomeriza

SUBMITTER: Xian Y 

PROVIDER: S-EPMC7176140 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature