This chapter provides a short review of various biophysical experiments that have been applied to the inhibitor of kappa B, IkBa and its binding partner, nuclear factor kappa B, or NFkB. The picture that emerges from amide hydrogen/deuterium exchange, NMR and binding kinetics experiments is...

Nucleocapsid proteins are the molecular jacks‑of‑all‑trades of small RNA viruses because they play pivotal roles in viral genomic RNA selection and packaging, regulate genome replication and virus budding and at the same time orchestrate a complex, dynamic interaction network with host...

Receptor‑mediated signaling plays an important role in health and disease. Recent reports have revealed that many proteins that do not adopt globular structures under native conditions, thus termed intrinsically disordered, are involved in cell signaling. Intriguingly, physiologically...

Linker histones are multi‑domain nucleosome binding proteins that stabilize higher order chromatin structures and engage in specific protein‑protein interactions. Here we emphasize the structural and functional properties of the linker histone C‑terminal domain (CTD), focusing on its...

Surprisingly few transcription factors drive animal development relative to the number and diversity of final tissues and body structures. Therefore, most transcription factors must function in more than one tissue. In a famous example, members of the Hox transcription factor family are...

In this chapter, I focus on the biochemical and structural characterization of the complex between the intrinsically disordered C‑terminal domain of the measles virus nucleoprotein (NTAIL) and the C‑terminal X domain (XD) of the viral phosphoprotein (P). I summarize the main experimental...

Intrinsically disordered proteins (IDPs) are widespread in eukaryotic proteomes and challenge the classical structure‑function paradigm that equates a folded 3‑D structure with protein function. However, IDPs often function by molecular recognition, in which they bind a partner molecule...

Some historical background is given for appreciating the impact of the empirical construct known as the cellular protein‑protein interactome, which is a seemingly de novo entity that has arisen of late within the context of postgenomic systems biology. The approach here builds on a...

An emerging class of disordered proteins underlies the elasticity of many biological tissues. Elastomeric proteins are essential to the function of biological machinery as diverse as the human arterial wall, the capture spiral of spider webs and the jumping mechanism of fleas. In this chapter,...

Interactions between Intrinsically Disordered Protein Regions (IDRs) and their targets commonly exhibit localised contacts via target‑induced disorder to order transitions. Other more complex IDR target interactions have been termed “fuzzy” because the IDR does not form a well‑defined...

It is now widely recognized that intrinsically disordered (or unstructured) proteins (IDPs, or IUPs) are found in organisms from all kingdoms of life. In eukaryotes, IDPs are highly abundant and perform a wide range of biological functions, including regulation and signaling. Despite increased...