Andy LiWang

This study identifies a conformational switch in KaiA that regulates the day-night transition in cyanobacterial clocks and shows its role in maintaining rhythmicity.

The paper identifies cold-sensitive protein conformational changes across the proteome using mass spectrometry in E. coli.

This study reconstitutes the cyanobacterial circadian clock in synthetic vesicles, showing that protein levels and vesicle size affect clock fidelity, with a mathematical model explaining how cyanobacteria maintain synchrony.

This study investigates how temperature affects the fold-switching mechanism of KaiB, a circadian clock protein, showing that proline isomerization is a rate-limiting step.

The paper uses Bayesian modeling to show that ultrasensitivity in KaiC phosphorylation, driven by differential KaiA binding to ATP/ADP states, enables metabolic compensation in the cyanobacterial circadian clock.