Conformation-Dependent Influences of Hydrophobic Amino Acids in Two In-Register Parallel β-Sheet Amyloids, an α-Synuclein Amyloid and a Local Structural Model of PrP^Sc.

ABSTRACT: Prions are unconventional pathogens that encode the pathogenic information in conformations of the constituent abnormal isoform of prion protein (PrP^Sc), independently of the nucleotide genome. Therefore, conformational diversity of PrP^Sc underlies the existence of many prion strains and species barriers of prions, although the conformational information is extremely limited. Interestingly, differences between polymorphic or species-specific residues responsible for the species/strain barriers are often caused by conservative replacements between hydrophobic amino acids. This implies that subtle differences among hydrophobic amino acids are significant for PrP^Sc structures. Here we analyzed the influence of different hydrophobic residues on the structures o

SUBMITTER: Otaki H 

PROVIDER: S-EPMC9453792 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature