Professional Overview
Honors and Awards
- Ruth McLean Bowman Bowers Excellence in Research Award, Baylor College of Medicine (2011)
- Keck Fellow, NIH Nanobiology Training Program (2007)
Professional Education
| Doctor of Philosophy: | Baylor College Of Medicine (2009) |
| Bachelor of Science: | Fudan University, Physics (2004) |
Stanford Advisors
| Michael Levitt: | Postdoctoral Faculty Sponsor |
Scientific Focus
Current Research Interests
One of my major interests is to solve structures of biological macromolecular complexes using an experimental technique called cryo electron-microscopy (cryo-EM). I have solved the structures of a protein-folding machine called Mm-cpn chaperonin at different states ranging from 4-10Å resolutions. These structures of chaperonins help us better understand their functions in preventing protein misfolding. This can eventually help people treat protein-misfolding diseases such as Alzimers, Parkinsons, etc.
I have also worked on automating the cryo-EM data acquisition in collaboration with engineers at JEOL (an electron microscope company). The end product - JADAS software system will simplify and expedite the data acquisition process and make cryo-EM readily accessible to the general field of biology.
My recent interest is to develop a computational method to model dynamics of large protein machineries and use this dynamic information to solve their three-dimensional cryo-EM structures.
Publications
- Multiscale natural moves refine macromolecules using single-particle electron microscopy projection images. Proc Natl Acad Sci U S A. 2012; (25): 9845-50
- Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber. Cell. 2011; (2): 240-52
- Mechanism of folding chamber closure in a group II chaperonin. Nature. 2010; (7279): 379-83
- Cryo-EM model validation using independent map reconstructions. Protein Sci. 2013
- Cryo-EM structure of a molluscan hemocyanin suggests its allosteric mechanism. Structure. 2013; (4): 604-13
- Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure. Structure. 2011; (5): 633-9
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