Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entirely or
partly and play important roles in diverse biological phenomena. Their structure dynamically …

Intrinsically disordered (ID) regions of proteins are recognized to be involved in biological
processes such as transcription, translation, and cellular signal transduction. Despite the …

Intrinsically disordered proteins (IDPs) play crucial roles in cellular processes and hold
promise as drug targets. However, the dynamic nature of IDPs remains poorly understood …

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 and regions (IDPs and IDRs) have attracted increasing
interest with their abundance in the human proteome and critical roles in various human …

Intrinsically disordered proteins (IDPs) are notoriously challenging to study both
experimentally and computationally. The structure of IDPs cannot be described by a single …

Highlights•Recent successes of artificial intelligence (AI) and machine learning (ML)
techniques can be leveraged to obtain quantitative insights into how intrinsically disordered …

Intrinsically disordered proteins (IDPs), which lack persistent structure, are a challenge to
structural biology due to the inapplicability of standard methods for characterization of folded …

Intrinsically disordered proteins (IDPs) constitute a significant fraction of eukaryotic
proteomes. High-resolution characterization of IDP conformational ensembles can help …

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