Post-translational modifications (PTMs) produce significant changes in the structural
properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes …

Proteins are the major component of the living cell. They play crucial roles in the
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

Research of a past decade and a half leaves no doubt that complete understanding of
protein functionality requires close consideration of the fact that many functional proteins do …

This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …

The abundant existence of proteins and regions that possess specific functions without
being uniquely folded into unique 3D structures has become accepted by a significant …

Traditionally, protein–protein interactions were thought to be mediated by large, structured
domains. However, it has become clear that the interactome comprises a wide range of …

Motivation: Intrinsically disordered regions are key for the function of numerous proteins, and
the scant available experimental annotations suggest the existence of different disorder …

Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions
because disordered segments permit interaction with several proteins and hence the re-use …

Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structures under
physiological conditions in vitro. They are highly abundant in nature and their functional …