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 discovery of intrinsically disordered proteins (IDP)(ie, biologically active proteins that do
not possess stable secondary and/or tertiary structures) came as an unexpected surprise, as …

Motivation: A sizeable fraction of eukaryotic proteins contain intrinsically disordered regions
(IDRs), which act in unfolded states or by undergoing transitions between structured and …

Many gene defects are relatively easy to identify experimentally, but obtaining information
about the effects of sequence variations and elucidation of the detailed molecular …

Intrinsic disorder is relatively common in proteins, plays important roles in numerous cellular
activities, and its prevalence was implicated in various human diseases. However …

Availability of computational methods that predict disorder from protein sequences fuels
rapid advancements in the protein disorder field. The most accurate predictions are usually …

Motivation: Intrinsically disordered proteins play a crucial role in numerous regulatory
processes. Their abundance and ubiquity combined with a relatively low quantity of their …

Introduction Intrinsic disorder prediction field develops, assesses, and deploys
computational predictors of disorder in protein sequences and constructs and disseminates …

Intrinsically disordered/unstructured proteins exist without a stable three-dimensional (3D)
structure as highly flexible conformational ensembles. The available genome sequences …

Intrinsically disordered proteins (IDPs) are either entirely disordered or contain disordered
regions in their native state. IDPs were found to be abundant in complex organisms and …