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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 ”@ |
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 |
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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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