Research focus
Many proteins require molecular chaperones to assume their native conformation in the cell. Our structures show how chaperones, AAA+ disaggregases and amyloid filaments act in protein homeostasis and neurodegenerative disease.
Hsp90, Hsp60 & CHIP
Cochaperones that recognize the client maturation state, and chaperonins that fold newly imported mitochondrial proteins.
Read more →AAA+ disaggregases & p97
Hexameric ATPases that couple ATP hydrolysis to polypeptide translocation through a central channel.
Read more →Tau & α-synuclein
Cryo-EM structures of disease-specific tau and α-synuclein folds from patient brain, and the PET ligands that bind them.
Read more →Nitric oxide synthase
How calmodulin and domain motions direct electron transfer in the nitric oxide synthase holoenzyme.
Read more →Recent publications
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