Adam Zlotnick

The paper develops and validates a method to quantify dynamic protein binding pockets using the HBV capsid assembly modulator site as a model, demonstrating robust performance across conformational states.

The paper uses a kinetic Monte Carlo model to simulate how CAMs alter HBV capsid assembly, revealing mechanisms that lead to noninfectious structures.

This study compares the binding of CAMs to two forms of HBV capsid protein, showing structural differences in CAM site adaptation between assembly-active and -inactive forms.

The paper determines the structures of mature HBV and Duck HBV, revealing that DNA forms a spool within the capsid that interacts with interior charges and creates a metastable state for genome uncoating.

This study investigates how the ratio of nucleic acid to SARS-CoV-2 N-protein affects liquid-liquid phase separation (LLPS) and finds that a 1:1 ratio maximizes condensate formation.