 Lysozyme is among the naturally occurring proteins known to form amyloid fibers under experimental conditions, and both natively alpha-strand region and the mutation site fall within the larger region identified as the core of lysozyme amyloid fibrillogenesis.A mechanism for direct alpha sheet and beta sheet interconversion has also been suggested, based on peptide plane flipping in which the αRαL dipeptide inverts to produce a ββ dihedral angle conformation.This process has also been observed in simulations of transthyretin and implicated as occurring naturally in certain protein families by examination of their dihedral angle conformations in crystal structures.