Year: 2019
Type: book-chapter
Abstract: Folding or misfolding. A – unfolded form of polypeptide B – spherical micelle as the result of water environment influence (path 1), C,D,E – different forms of locally discordant spherical micelle, F – amyloid form with linear propagation of bands of different hydrophobicity level (low influence of water environment –path 2). Path 3 – possible transformation of globular form to amyloid form. Dashed line – path not observed however the search of reverse transformation highly expected for therapy. Schematic depiction of alternative folding pathways, depending on the influence of the aqueous environment. Path 1: transition between the unfolded structure (A) and an ordered form conditioned by the influence of water (micelle-like structure; B) Path 2: weak influence of the external force field results in the folding process being dominated by the intrinsic properties of each residue, and – consequently – in linear propagation of bands characterized by variable hydrophobicity (F) Path 3: amyloid transformation resulting from a decrease in the influence of the aqueous environment. Path 3 (dashed line): hypothetical reverse transformation of an amyloid form into a globular form. C, D, E – various local deformations in the structure of a micellar hydrophobic core. G, H, I – various linear patterns depending on the sequence of the polypeptide. This chapter discusses the potential for structural transformation represented by the dashed line (reverse path 3).
Source: Elsevier eBooks
Authors: Leszek Konieczny, Irena Roterman
Institution: Jagiellonian University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
OpenAlex ID: W2980102548