Dr. Lila Gierasch is a biophysical chemist recognized for her work on protein folding,
with particular emphasis on in vivo folding and roles of molecular chaperones. Her
lab has addressed protein folding in cells, developing tools to study the fate of
newly synthesized proteins, including their proper folding and cellular localization.
She and her co-workers elucidated conformational propensities and physical properties
of signal sequences, which helps to explain how diverse sequences can target a polypeptide
chain to the secretory pathway. Gierasch’s lab has a long-time interest in the roles
of molecular chaperones, a network of species that protect incompletely folded proteins
in the cell from aggregation and misfolding. They seek to understand how molecular
chaperones recognize ‘unfoldedness’ in their protein substrates. She showed that chaperonins
like GroEL exploit hydrophobic surfaces to recognize substrates, while Hsp70s bind
polypeptides as extended chains. Recently, Lila Gierasch’s laboratory has unraveled
the allosteric mechanism of Hsp70 chaperones, which are central hubs in protein homeostasis
and quality control. The work of her laboratory provides insights into the pathologies
that arise from mistakes in protein folding, such as the neurodegenerative diseases.
Gierasch has been the recipient of several awards and is currently Editor-in-Chief
of the Journal of Biological Chemistry. She is a member of both the American Academy
of Arts and Sciences and the National Academy of Sciences.