G. A. Pellowe

Mechanism of chaperone coordination during cotranslational protein folding in bacteria

The paper investigates how chaperones coordinate during cotranslational protein folding in bacteria, showing they create a protected space for maturation without destabilizing intermediates.

Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter

The paper uses HDX-MS, mutagenesis, and MD simulations to show that substrate binding and protonation drive conformational changes in a transporter, while inhibitors prevent this transition.