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

Despite the wealth of knowledge gained about intrinsically disordered proteins (IDPs) since
their discovery, there are several aspects that remain unexplored and, hence, poorly …

At the turn of the twenty-first century, fundamental changes took place in the understanding
of the structure and function of proteins and then in the appreciation of the intracellular …

Intrinsic disorder is instrumental for a wide range of protein functions, and its analysis, using
computational predictions from primary structures, complements secondary and tertiary …

Proteins with intrinsically disordered regions (IDRs) are common among eukaryotes. Many
IDRs interact with nucleic acids and proteins. Annotation of these interactions is supported …

Dysregulation of protein–protein interactions (PPIs) commonly leads to disease. PPI
stabilization has only recently been systematically explored for drug discovery despite being …

With the increased focus on intrinsically disordered proteins (IDPs) and their large
interactomes, the question about their specificity—or more so on their multispecificity—arise …

A good portion of the 'protein universe'embodies the 'dark proteome'. The latter comprises
proteins not amenable to experimental structure determination by existing means and …

Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined
three-dimensional structure. Conformational changes in intrinsically disordered regions of a …

Advanced age represents one of the major risk factors for Parkinson's Disease. Recent
biomedical studies posit a role for microRNAs, also known to be remodelled during ageing …