Conspectus Are all protein interactions fully optimized? Do suboptimal interactions
compromise specificity? What is the functional impact of frustration? Why does evolution not …

Advances in the characterization of intrinsically disordered proteins (IDPs) have unveiled a
remarkably complex and diverse interaction landscape, including coupled folding and …

Amyloid fibrils are highly stable misfolded protein assemblies that play an important role in
several neurodegenerative and systemic diseases. Although structural information of the …

Biological life depends on motion, and this manifests itself in proteins that display motion
over a formidable range of time scales spanning from femtoseconds vibrations of atoms at …

Transcription depends on complex networks, where folded hub proteins interact with
intrinsically disordered transcription factors undergoing coupled folding and binding. For …

Recognition motifs that mediate protein–protein interactions are usually embedded within
longer intrinsically disordered regions. While binding interfaces involving the recognition …

Intrinsically disordered proteins (IDPs) can be generally described as a class of proteins that
lack a well-defined ordered structure in isolation at physiological conditions. Upon binding to …

The basic zippers (bZIPs) are one of two large eukaryotic families of transcription factors
whose DNA binding domains are disordered in isolation but fold into stable α-helices upon …

Protein–protein associations are often mediated by an intrinsically disordered protein region
interacting with a folded domain in a coupled binding and folding reaction. Classic physical …

By merging advanced dimensionality reduction (DR) and clustering algorithm (CA)
techniques, our study advances the sampling procedure for predicting NMR chemical shifts …