My research focused on molecular chaperones that degrade and remodel client proteins. Molecular chaperones play central roles in development and cell cycle. The decline in the function of molecular chaperones correlates with many pathological conditions, including neurodegenerative diseases. I am especially interested in how different molecular chaperones recognize and engage their respective targets and use the energy of ATP hydrolysis to guide protein folding or unfolding. I am exploiting a variety of structural biology, microscopy, and biochemical methods to address these questions.

“Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate” X. Fei,

T. A. Bell, S. Jenni, B.M. Stinson, T.A. Baker, S.C. Harrison, and R.T. Sauer Elife 9, e52774

(2020)

“Structural basis of ClpXP recognition and unfolding of ssrA-tagged C-degron substrates”

X. Fei, T. A. Bell, S. R. Barkow, T. A. Baker, R. T. Sauer biorxiv doi: https://doi.org/10.1101/

2020.05.07.082636 (2020) 

“Formation and Structures of GroEL:GroES2 Chaperonin “Footballs”, the Protein Folding

Functional Form”, X. Fei, X. Ye, N. La Ronde-LeBlanc, G.H. Lorimer, Proceedings of the

National Academy of Sciences 111 (35), 12775-80 (2014)

“Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å

resolution”, X. Fei, D. Yang, N. La Ronde-LeBlanc, G.H. Lorimer, Proceedings of the

National Academy of Sciences 110 (32), E2958-E2966 (2013)