Intrinsically disordered proteins (IDPs) are widely distributed across eukaryotic cells, playing
important roles in molecular recognition, molecular assembly, post-translational …

Intrinsically disordered proteins (IDPs) are proteins that perform important biological
functions without well‐defined structures under physiological conditions. IDPs can form …

Epigallocatechin gallate (EGCG) from green tea can induce apoptosis in cancerous cells,
but the underlying molecular mechanisms remain poorly understood. Using SPR and NMR …

Intrinsically disordered proteins (IDPs) frequently mediate phase separation that underlies
the formation of a biomolecular condensate. Together with theory and experiment, efficient …

Molecular dynamics (MD) simulation is widely used to complement ensemble-averaged
experiments of intrinsically disordered proteins (IDPs). However, MD often suffers from …

Intrinsically disordered proteins (IDPs) play important roles in cellular functions. The inherent
structural heterogeneity of IDPs makes the high-resolution experimental characterization of …

Machine learning has achieved remarkable success across a broad range of scientific and
engineering disciplines, particularly its use for predicting native protein structures from …

Intrinsically disordered proteins (IDPs) are proteins that lack rigid 3D structure. Hence, they
are often misconceived to present a challenge to Anfinsen's dogma. However, IDPs exist as …

Replica exchange with solute tempering (REST) is a highly effective variant of replica
exchange for enhanced sampling in explicit solvent simulations of biomolecules. By scaling …

Intrinsically disordered proteins (IDPs) are over-represented in major disease pathways and
have attracted significant interest in understanding if and how they may be targeted using …