LAUSR

The secondary structure of poly(amino acids) is a major factor for controlling and understanding the functionality and properties of proteins. Investigations on model-homo-polyaminoacids represent an important contribution to understand folding or proteins. In this perspective article we discuss the secondary structure formation of the homopolymers of oligo- and poly-glutamic acid (Glu), aspartic acid (Asp) and α-aminoisobutyric acid (Aib). We review information on external and internal factors, such as the nature of side groups, interactions with solvents and interactions between chains. A major focus is directed on understanding the folding of poly(amino acids) and the influence of functional groups in their folding behaviour, especially in hybrid-polymers consisting of oligo(amino acids) and synthetic polymers. Being part of the SFB TRR 102 "Polymers under multiple constraints: restricted and controlled molecular order and mobility" our results and this overview are embedded into the crosssection of protein fibrillation and supramolecular polymers. Analyzing polymer- and amino acid folding is an important step for the utilization and design of future biomolecules and understanding the principles governing amyloid fibrillation. This article is protected by copyright. All rights reserved.