Single Protein Conformational Dynamics: Folding, Binding, and Aggregation of Disordered Proteins
We study conformational dynamics of proteins using single molecule Förster resonance energy transfer (FRET) spectroscopy. Especially, we focus on intrinsically disordered proteins (IDPs) that are closely related to various human diseases. The primary goal of our research is to understand the mechanisms of binding and aggregation processes of IDPs.
- Understanding binding mechanism of IDPs. We try to understand the mechanistic details of binding: how molecular conformations evolve when two molecules approach to each other, make a contact, and form a bound complex. This information is contained in the moment of binding that can be probed only by single molecule spectroscopy.
- Characterization of the early stage of aggregation. Protein or peptide oligomers are thought to be implicated in the development of various neurodegenerative diseases. However, oligomerization has been extremely difficult to study due to the heterogeneity of the process. Single molecule spectroscopy can effectively characterize this complicated process by detecting individual oligomers without separation.
Fast single-molecule FRET spectroscopy: theory and experiment
Postdoctoral positions are available. To apply email a CV, bibliography, brief summary of research accomplishments, and the names of references.
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