Fig. 2: Conformation ensemble and interpeptide interactions of the gal-3 225–250 aggregate.
From: Atypical β-strand insertion mediates the noncovalent cross-linking in amyloid aggregates
Representative STM images (a) and structural models for each conformational substate of gal-3 225–250 (b). Scale bar: 2 nm. Gray: conformations with no cross-β-strand linker. Blue and red indicate the proportion without and with the cross-β-strand linker, respectively. c The inter-conformational interactions involving the cross-β-strand linker (red) within the gal-3 225–250 aggregates relative to the total interactions (overall). d Representative STM images of inter-conformational interactions. White boxes highlight the cross-β-strand linker-mediated interpeptide interactions. Scale bars: 3 nm. STM experiments were independently repeated using different samples and tips. At least three high-resolution STM images (60 × 60 nm) were acquired for each sample. Source data are provided as a Source data file.
