Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …

The past decade has witnessed great advances in our understanding of protein structure‐
function relationships in terms of the ubiquitous existence of intrinsically disordered proteins …

A significant fraction of every proteome is occupied by biologically active proteins that do not
form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and …

Proteins, with their seemingly limitless functional diversity, are major players in the
maintenance of life. The ability of proteins to fulfill these various biological functions is …

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 …

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 …

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) carry out many biological functions. They lack a
stable three-dimensional structure, but rather adopt many different conformations in dynamic …

Proteins may vary from being rigid to having flexible regions to being completely disordered,
either as an intrinsically disordered protein (IDP) or having specific intrinsically disordered …

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 …