Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …

Accurate predictions of the three-dimensional structures of proteins from their amino acid
sequences have come of age. AlphaFold, a deep learning-based approach to protein …

Predicting the binding structure of a small molecule ligand to a protein--a task known as
molecular docking--is critical to drug design. Recent deep learning methods that treat …

Protein structures can provide invaluable information, both for reasoning about biological
processes and for enabling interventions such as structure-based drug development or …

Most proteins fold into 3D structures that determine how they function and orchestrate the
biological processes of the cell. Recent developments in computational methods for protein …

Intrinsically disordered proteins and protein regions (IDPs/IDRs) exist without a single well-
defined conformation. They carry out important biological functions with multifaceted roles …

Identification of intrinsic disorder in proteins relies in large part on computational predictors,
which demands that their accuracy should be high. Since intrinsic disorder carries out a …

The MobiDB database (URL: https://mobidb. org/) is a knowledge base of intrinsically
disordered proteins. MobiDB aggregates disorder annotations derived from the literature …

The AlphaFold Protein Structure Database contains predicted structures for millions of
proteins. For the majority of human proteins that contain intrinsically disordered regions …

Intrinsically disordered proteins and protein regions make up a substantial fraction of many
proteomes in which they play a wide variety of essential roles. A critical first step in …