Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical
reactions are executed inside of biomolecular condensates formed by ultradynamic …

Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …

IUPred2A is a combined prediction tool designed to discover intrinsically disordered or
conditionally disordered proteins and protein regions. Intrinsically disordered regions exist …

Proteins undergoing liquid–liquid phase separation are being discovered at an increasing
rate. Since at the high concentrations present in the cell most proteins would be expected to …

Abstract The Protein Ensemble Database (PED)(https://proteinensemble. org), which holds
structural ensembles of intrinsically disordered proteins (IDPs), has been significantly …

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

Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of
intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This …

Highlights•Sparsely populated protein states can play significant biological roles.•NMR
spectroscopy can structurally and dynamically characterize 'invisible'protein states.•We …

Transcription activation domains (ADs) are inherently disordered proteins that often target
multiple coactivator complexes, but the specificity of these interactions is not understood …

Studying the conformational landscape of intrinsically disordered and partially folded
proteins is challenging and only accessible to a few solution state techniques, such as …