Abstract

Post-translational modifications play a crucial role in modulating the structure and function of proteins. Myristoylation, the attachment of a myristoyl group to the N-terminus of a protein, is a common modification that facilitates membrane association. While the effects of myristoylation on structured proteins have been extensively studied, its impact on intrinsically disordered proteins (IDPs) remains less explored. This abstract highlights the changes in structure and hydration of myristoylated IDPs. Intrinsically disordered proteins are a class of proteins that lack a well-defined structure but possess critical biological functions. Myristoylation can induce structural changes in IDPs by promoting the formation of transient secondary structure elements or modulating local folding propensity. The myristoyl group's presence can alter the conformational dynamics of IDPs, resulting in the adoption of specific structural motifs upon membrane binding. Additionally, myristoylation can facilitate protein-protein interactions, leading to changes in the overall structure of IDPs. Hydration, an essential factor for protein stability and function, is also affected by myristoylation in IDPs. Experimental studies have shown that myristoylated IDPs exhibit distinct hydration dynamics compared to their non-myristoylated counterparts. The myristoyl group can influence the hydration of specific regions of the IDP by shielding them from solvent exposure, while other regions may experience enhanced hydration. These hydration changes have implications for the interactions of myristoylated IDPs with partner proteins and membranes.