Mazdak Khajehpour

This study investigates the mechanism by which Eag chaperones release effector transmembrane domains using biochemical, biophysical, and structural approaches.

The paper quantifies ion binding to biomolecular condensates using NMR and shows that ion uptake follows water affinity matching, affecting condensate microenvironment and biochemical processes.

This paper shows that the phage protein paratox is intrinsically disordered in dilute solution but folds into a globular structure when bound to ComR or in the presence of stabilizing solutes.