Characterization of Intrinsically Disordered Alpha-Synuclein Protein in Solution

조회수 : 287 등록일 : 2017.10.16 20:55

일시 : 2017.10.11 17:00
소속 : 서울대학교 화학부
발표자 : 이정호
장소 : RA204
Intrinsically disordered proteins (IDPs) are functional despite the lack of well-defined structures. Their structural plasticity endows functional flexibility, and an IDP can interact with various binding partners by adopting different conformations. Despite the fact that IDPs are prevalent in the eukaryotic proteome, they are much less explored compared to well-ordered proteins, necessitating the development of new analytical techniques to investigate IDPs. In this presentation, I will present recent experimental approaches to characterize the conformational space sampled by IDPs in solution. In particular, NMR methods to quantitatively describe backbone torsion angles of IDPs will be presented. a-Synuclein protein will be employed as a model IDP, whose aggregation is closely related to the pathogenesis of Parkinson’s disease. Since the function of a-synuclein is closely linked to its ability to interact with lipid membranes, efforts to monitor this interaction will be discussed. Finally, future directions of my research regarding IDP aggregation will be introduced.
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