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

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

Artificial intelligence-based protein structure prediction methods such as AlphaFold have
revolutionized structural biology. The accuracies of these predictions vary, however, and …

There has been an exponential increase in the design of synthetic antimicrobial peptides
(AMPs) for its use as novel antibiotics. Synthetic AMPs are substantially enriched in residues …

Many fungi and oomycete species are devasting plant pathogens. These eukaryotic
filamentous pathogens secrete effector proteins to facilitate plant infection. Fungi and …

Molecular dynamics (MD) simulations have become increasingly useful in the modern drug
development process. In this review, we give a broad overview of the current application …

Intrinsically disordered regions (IDRs) are ubiquitous across all domains of life and play a
range of functional roles. While folded domains are generally well-described by a stable 3D …

Many diseases are driven by proteins that are aberrantly ubiquitinated and degraded. These
diseases would be therapeutically benefited by targeted protein stabilization (TPS). Here we …

Recognition of the natural abundance and functional importance of intrinsically disordered
proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions …

Protein intrinsic disorder is found in all kingdoms of life and is known to underpin numerous
physiological and pathological processes. Computational methods play an important role in …