Traditional conventions that a protein’s sequence dictates its definitive, tertiary structure, and that this fixed structure provides the protein with the ability to carry out its designated role(s) are still correct but not for all proteins. Research over the past decade discovered that several key proteins possess intrinsically disordered regions (IDRs) that are crucial to their ability to perform specific functions and are observed clustered together within important classes of proteins. In this review, we aim to demonstrate how free energy landscapes, molecular dynamics simulations, and homology modeling are helpful in understanding key conformational dynamics of intrinsically disordered proteins (IDPs). Additionally, we use a list of predicted IDPs found in Arabidopsis to identify chromatin organizers and transcriptional regulators as being highly enriched in IDPs. Furthermore, we focus our attention to specific proteins within these families such as HAC5, EFS, ANAC019, ANAC013, and ANAC046. Future studies are needed to experimentally identify additional IDPs and their binding mechanisms.