10.6084/m9.figshare.c.3642779_D2.v1
Bruno Macedo
Bruno
Macedo
Ricardo SantâAnna
Ricardo
SantâAnna
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 PrP23â231 is shown, along with the corresponding spectral bands assigned to different secondary structure components.