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 …

This review presents the potential for application of computational tools in peptide science
based on a sample BIOPEP database and program as well as other programs and …

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

Motivation Capturing long-range interactions between structural but not sequence neighbors
of proteins is a long-standing challenging problem in bioinformatics. Recently, long short …

Protein intrinsic disorder is becoming increasingly recognized in proteomics research. While
lacking structure, many regions of disorder have been associated with biological function …

Motivation Related to many important biological functions, intrinsically disordered regions
(IDRs) are widely distributed in proteins. Accurate prediction of IDRs is critical for the protein …

To explore the mechanisms and evolution of cell-cycle control, we analyzed the position and
conservation of large numbers of phosphorylation sites for the cyclin-dependent kinase …

Abstract Background Intrinsically unstructured proteins (IUPs) lack a well-defined three-
dimensional structure. Some of them may assume a locally stable structure under specific …

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 …

Intrinsically disordered proteins and regions are widely distributed in proteins, which are
associated with many biological processes and diseases. Accurate prediction of intrinsically …