일시 : 2017년 4월 5일(수) 오후5시-7시

장소 : 과학관 604호

연사 : 이정호 교수님(서울대, 화학부)

​

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 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 and amyloid-b proteins will be shown as model IDPs, whose aggregation are closely related to the pathogenesis of Parkinson’s and Alzheimer’s disease, respectively. 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 presented.

​