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| Name |
Gierasch, Lila M. |
| Location
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University of Massachusetts at Amherst |
| Primary Field
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Biochemistry |
| Secondary Field
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Biophysics and Computational Biology |
 Election Citation
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Gierasch pioneered the use of spectroscopy methods that can study the fate of newly synthesized proteins, including their folding, interactions with chaperones, and cellular localization.
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Research Interests
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Lila Gierasch's laboratory has made fundamental contributions to the relationship between amino acid sequence and the preferred conformations of peptides and proteins. Her work shed light on turn propensities in proteins and offered a basis for design of analogues of bioactive peptides. 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. Her lab 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 and coworkers were involved in studies that demonstrated the roles of molecular chaperones, a network of species that protect incompletely folded proteins in the cell from aggregation and misfolding. Her lab described how molecular chaperones recognize 'unfoldedness' in their protein substrates, showing 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. |
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