Molecular Chaperones and Aggregation

Space-filling model of large protein with smaller protein bound to it
Data from cross-linking mass spectrometry (XL-MS) leads to this predicted model of binding between DnaJC7, a molecular chaperone (grayscale), and a fragment of tau protein (yellow).

A major focus of our work is molecular chaperones – proteins that bind to proteins and alter their conformation. Dysfunction of chaperones or their substrate proteins is associated with many human diseases, so understanding how proteins and their chaperones recognize and interact with each other is fundamental in discerning the mechanisms underlying neurodegenerative diseases.

We are particularly interested in chaperones’ interactions with tau and other proteins that form amyloid fibrils. Our ultimate goal is controlling protein aggregation in neurodegenerative diseases.

We employ a variety of analytic techniques to uncover kinetics, structure, and biochemistry, to understand how chaperones bind to amyloidogenic proteins and regulate their ability to assemble.