报告简介: A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in-vitro, exposing new mechanistic details that are now calling for quantitative in-vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein SOD1 in vitro and in transgenic mice. The results, based on tissue sampling by quantitative antibody assays, show that the SOD1 fibrillation kinetics in vitro mirrors with remarkable accuracy the spinal-cord aggregate build-up and disease progression in transgenic mice. This similarity between in-vitro and in-vivo data suggest that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology, prion-like infectivity and organism-level protein-aggregation phenomena in general.
报告题目:Folding and structural properties of proteins:things that the experimentalist needs to know
报告人：瑞典皇家科学院院士 Mikael Oliveberg 教授
报告简介：This talk is about the generic properties, folding and conformational behaviour of proteins.For example, how do proteins respond to point mutations and denaturants, and how can this be used to the advantage of the experimentalist.The talk will also outline some new protein-design strategies for uncovering structural dynamics and cooperative transitions that elude standard analysis.