Solvent-induced tuning of internal structure in a protein amyloid protofibril.

ABSTRACT: An important goal in studies of protein aggregation is to obtain an understanding of the structural diversity that is characteristic of amyloid fibril and protofibril structures at the molecular level. In this study, what to our knowledge are novel assays based on time-resolved fluorescence anisotropy decay and dynamic quenching measurements of a fluorophore placed at different specific locations in the primary structure of a small protein, barstar, have been used to determine the extent to which the protein sequence participates in the structural core of protofibrils. The fluorescence measurements reveal the structural basis of how modulating solvent polarity results in the tuning of the protofibril conformation from a pair of parallel β-sheets in heat-induced protofibrils to a single par

SUBMITTER: Jha A 

PROVIDER: S-EPMC3443786 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature