It is now increasingly evident that a large fraction of the human proteome comprises proteins
that, under physiological conditions, lack fixed, ordered 3D structures as a whole or have …

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 …

Crowding caused by the high concentrations of macromolecules in the living cell changes
chemical equilibria, thus promoting aggregation and folding reactions of proteins. The …

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 …

Over the last two decades, it has become increasingly clear that a large fraction of the
human proteome is intrinsically disordered or contains disordered segments of significant …

Biologically active but floppy proteins represent a new reality of modern protein science.
These intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered and …

Many proteins and protein segments cannot attain a single stable three-dimensional
structure under physiological conditions; instead, they adopt multiple interconverting …

Intrinsically disordered proteins (IDPs) are an important class of functional proteins that is
highly prevalent in biology and has broad association with human diseases. In contrast to …

Intrinsically disordered proteins (IDPs) are important components of the cellular signalling
machinery, allowing the same polypeptide to undertake different interactions with different …

Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …