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Chinese      

Education and Experience:

2003-now : Assistant Research Fellow

                     Institute of Biological Chemistry, Academia Sinica

1999-2003 : Postdoctoral Fellow

                     Institute of Chemistry, Academia Sinica

1993-1998 : Ph. D.

                     Department of Biochemistry, University of Cambridge, UK

1992-1993 : Research Assistant

                     Institute of Biological Chemistry, Academia Sinica

1989-1991 : M. Sc.

                     Institute of Biochemical Sciences, National Taiwan University

1985-1989 : B. S.

                     Department of Agricultural Chemistry, National Taiwan University

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Research interest:

My research interest is regarding protein folding and misfolding behaviors in order to answer how proteins can fold into its native structure and how certain proteins can misfold and cause disease.  Studies about protein folding are mainly the development of new methodologies to unravel the intrinsic properties of the protein folding process.  The misfolding studies focus on the mechanism of amyloid fibril formation, factors influencing molecular assembly, species barrier in prion disease, and designing inhibitor for amyloid formation. 

I.   Protein folding:  We propose a new method to study the early stage of protein folding.  Our idea is to add a photolabile cage to a small protein.  The protein is therefore unfolded due to the interference of the bulky cage.  The photolabile cage can be photolyzed quickly by 300-400 nm light irradiation.  After photolysis, the cage is released and the protein starts to refold.  The whole folding process will be recorded by fluorescence spectroscopy combined with a flash photolysis apparatus.

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  The scheme of the experimental design of our photolabile 
  caging strategy for exploring protein folding at early stage.

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II.  Protein misfolding: There are more than 20 diseases are caused by the formation of amyloid fibril due to protein misfolding.  The epidemic of mad cow disease happened in England in 1990”¦s received broad attention all over the world due to the suspicion that the prion disease might be transmitted from cattle to human.   We use prion peptide as our model system to explore the origin and mechanism of the structural transition and to study the ”„species barrier”¦ in the disease transmission.

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    EM image of the amyloid fibril formed from the prion peptide.

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