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.
Corrêa
Daniel Henrique do Amaral
DH
Institute of Chemistry and Instituto Nacional de Ciência e Tecnologia em Biologia Estrutural e Bioimagem, Brazil.
Ramos
Carlos Henrique Inácio
CH
D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000235:genetics; D000818:Animals; D001059:Apoproteins / Q000737:chemistry* / Q000235:genetics; D045744:Cell Line, Tumor; D002470:Cell Survival; D002942:Circular Dichroism; D051379:Mice; D016297:Mutagenesis, Site-Directed; D009154:Mutation / Q000235:genetics; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D017510:Protein Folding; D050661:Sperm Whale
D016229:Amyloid beta-Peptides; D001059:Apoproteins; D009211:Myoglobin; C010857:apomyoglobin