10.6084/m9.figshare.c.3642779_D2.v1 Bruno Macedo Bruno Macedo Ricardo Sant’Anna Ricardo Sant’Anna Susanna Navarro Susanna Navarro Yraima Cordeiro Yraima Cordeiro Salvador Ventura Salvador Ventura MOESM1 of Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria Springer Nature 2015 Mammalian prions Protein aggregation Protein conformation Inclusion bodies Amyloids E. coli 2015-11-04 05:00:00 Journal contribution https://springernature.figshare.com/articles/journal_contribution/MOESM1_of_Mammalian_prion_protein_PrP_forms_conformationally_different_amyloid_intracellular_aggregates_in_bacteria/4463438 Additional file 1. In the Supplemental Material Section the Amide I region of the ATRFTIR spectrum of purified native recombinant PrP23–231 is shown, along with the corresponding spectral bands assigned to different secondary structure components.