David Balchin

The paper identifies cyclic peptides that selectively bind to a cotranslational folding intermediate of β-galactosidase, revealing a druggable pocket formed during translation.

The paper investigates how chaperones like Hsp70, Hsp90, and TRiC bind to nascent p53 during translation, showing TRiC's specificity and how mutations affect this process.

The paper shows that the ribosome coordinates folding and assembly of a complex protein to enable efficient biogenesis.

This study investigates how GroEL/ES interacts with nascent proteins on ribosomes, showing that GroEL binds and destabilizes substrates, while GroES facilitates partial encapsulation and refolding.

The paper investigates how the human ribosome modulates multidomain protein folding by delaying domain docking, contrasting with bacterial ribosomes.

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