The Effect of Multisite Phosphorylation on the Conformational Properties of Intrinsically Disordered Proteins.

ABSTRACT: Intrinsically disordered proteins are involved in many biological processes such as signaling, regulation, and recognition. A common strategy to regulate their function is through phosphorylation, as it can induce changes in conformation, dynamics, and interactions with binding partners. Although phosphorylated intrinsically disordered proteins have received increased attention in recent years, a full understanding of the conformational and structural implications of phosphorylation has not yet been achieved. Here, we present all-atom molecular dynamics simulations of five disordered peptides originated from tau, statherin, and β-casein, in both phosphorylated and non-phosphorylated state, to compare changes in global dimensions and structural elements, in an attempt to gain more insight i

SUBMITTER: Rieloff E 

PROVIDER: S-EPMC8541499 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature