Abstract

To test the hypothesis that the ability to form ordered β-rich amyloid fibers with identical structures is a generic property of proteins we present a study on the overall structures of fibers formed by apomyoglobin mutants that either stabilize or destabilize the native state or the intermediate. Our results indicate that, at least at the macroscopic level, ordered β-rich amyloid fibers have similar structures.

Keywords: Amyloid fibrils, protein folding, site-directed mutagenesis, intermediate, apomyoglobin