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

Abstract Predicting three-dimensional (3D) protein structures has been challenging for
decades. The emergence of AlphaFold2 (AF2), a deep learning-based machine learning …

Intrinsically disordered proteins and regions (collectively, IDRs) are pervasive across
proteomes in all kingdoms of life, help to shape biological functions and are involved in …

Intrinsically disordered proteins (IDPs) perform a broad range of functions in biology,
suggesting that the ability to design IDPs could help expand the repertoire of proteins with …

Intrinsically disordered proteins and protein regions (IDPs/IDRs) carry out important
biological functions without relying on a single well-defined conformation. As these proteins …

Gene expression in Arabidopsis is regulated by more than 1,900 transcription factors (TFs),
which have been identified genome-wide by the presence of well-conserved DNA-binding …

Conformational heterogeneity is a defining hallmark of intrinsically disordered proteins and
protein regions (IDRs). The functions of IDRs and the emergent cellular phenotypes they …

Biomolecular nuclear magnetic resonance (NMR) spectroscopy and artificial intelligence
(AI) have a burgeoning synergy. Deep learning-based structural predictors have forever …

Conformational properties of intrinsically disordered proteins (IDPs) are governed by a
sequence-ensemble relationship. To differentiate the impact of sequence-local versus …

Intrinsically disordered proteins (IDPs) exhibit molecular-level conformational dynamics that
are functionally harnessed across a wide range of fascinating biological phenomena. The …