The long-term goal of our laboratory is to reveal the mechanism of the protein amyloidosis on the basis of complete characterization of the tertiary and quaternary structural features in static and dynamic states. In particular, we are interested in elucidating age-dependent structural transitions of proteins; determination of the ‘4-dimensional atomic-resolution structure’ of a protein would provide unprecedented insights regarding protein aging and aggregation mechanisms. In order to accomplish this goal, we target structural characterization of amyloidogenic proteins and chaperones, structural features of which are known to be affected by aging and to eventually cause various human diseases. Notably, we aim to conduct simultaneous and interactive studies regarding amyloidosis and its protection mechanisms, because we believe that this bilateral approach would provide novel and relevant information regarding the disease-related pathogenesis of amyloidogenic proteins. The specific aims of our laboratory include the following.
1. Characterization of the dynamic structural features of proteins
2. Elucidation of the pathogenesis mechanisms of amyloidogenic proteins
3. Elucidation of the interactions between chaperones and pathogenic aggregation-prone proteins
4. Development of novel therapeutic strategy based on structural understanding to amyloidosis mechanisms of proteins
Advisor Professor : Kim, Jin Hae
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