ABSTRACT
Fibrous proteins form long rod-or wire-like protein laments that are usually inert, water insoluble, and found as aggregates due to hydrophobic interactions between amino acid side chains. They often contain α-helix and β-sheet motifs as well as disulde bonds between chains. Examples of structural organization of brous proteins include “coiled coils” of α-helices (keratins), extended antiparallel β sheets (silk broin), and triple helical arrangements (collagen family).
