1P018 CryoEM structure of the flagellar filament of Salmonella FljB and implication of its difference from the FliC filament(Protein: Structure,Poster,The 52th Annual Meeting of the Biophysical Society of Japan(BSJ2014))

Abstract

We previously repoted that amyloid formation of Ab(25-35) peptide is strongly modified by soluble proteins with electrostatic interactions. An extension of this study was done for providing further insights into interactions between amyloidgenic and other soluble proteins, partly motivated by the question whether the interaction is observed for more pathologically important cases. The results gave some general aspects of the interaction by demonstrating several different modes of the interactions. It was, for example, indicated that distinction between specific and non-specific modes of the interactions are rather ambiguous, and some more important suggestions were also obtained.