Going through changes: effect of phosphoserine on secondary structure preference and dipole-dipole interactions in model peptides

Abstract

Intrinsically disordered proteins (IDPs) are enriched in polar and charged amino acids and lack a single, well-defined tertiary structure. IDPs are frequently the targets of post-translational modifications (PTMs) which can affect protein folding or stability, activity, susceptibility to degradation, and function. Phosphorylation is one of the most common PTMs and occurs on serine, threonine, and tyrosine residues. Hyperphosphorylation of some IDPs is associated with disease states, such as the tau protein in Alzheimer’s disease and α-synuclein in Parkinson’s disease.