Insights on the structure of amyloid fibrils from site-directed mutagenesis.

To test the hypothesis that the ability to form ordered beta-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 beta-rich amyloid fibers have similar structures.