Secondary Structure in Amyloids in Relation to Their Wild Type Forms.

ABSTRACT: The amyloid structures and their wild type forms, available in the PDB database, provide the basis for comparative analyses. Globular proteins are characterised by a 3D spatial structure, while a chain in any amyloid fibril has a 2D structure. Another difference lies in the structuring of the hydrogen bond network. Amyloid forms theoretically engage all the NH and C=O groups of the peptide bonds in a chain with two hydrogen bonds each. In addition, the hydrogen bond network is highly ordered-as perpendicular to the plane of the chain. The β-structure segments provide the hydrogen bond system with an anti-parallel system. The folds appearing in the rectilinear propagation of the segment with the β-structure are caused by just by one of the residues in the sequence-residues with a Rα-helical

SUBMITTER: Roterman I 

PROVIDER: S-EPMC9820225 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature