Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell. [PDF]
PLoS ONE, 2019 Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered residues in the sequence.
Antonio Deiana +3 more
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Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs) [PDF]
Chemical Reviews, 2014 It has long been axiomatic that a protein’s structure determines its function. Intrinsically disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure–function paradigm. They do not exhibit stable secondary and/or tertiary structures and exist as dynamic ensembles of interconverting conformers with preferred, nonrandom ...
Gary Pielak +2 more
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Biomolecules, 2022 The unique functions of intrinsically disordered proteins (IDPs) depend on their dynamic protean structure that often eludes analysis. High-speed atomic force microscopy (HS-AFM) can conduct this difficult analysis by directly visualizing individual IDP ...
Toshio Ando
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Polymer Concepts in Cellular Function. [PDF]
Adv Sci (Weinh)Advanced Science, EarlyView.
Yu M +7 more
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Adenosine triphosphate as a modulator of protein interactions and stability. [PDF]
FEBS Open BioATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Tan S, Curtis R.
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Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness [PDF]
MicrobiologyopenThe works examines the link between intrinsic disorder in bacterial protein structure, and bacterial function, and antimicrobial resistance. It highlights how flexible, disordered proteins support secretion, stress responses, desiccation protection, and virulence, while also suggesting that these adaptable regions may provide novel targets for ...
O' Callaghan J +3 more
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A Site-Aware Representation Learning Framework For Unified Molecular Interaction Modeling and Generative Design. [PDF]
Adv Sci (Weinh)MolDBG is a site‐aware, sequence‐only framework that unifies drug‐target affinity prediction, binding‐site identification, and affinity‐conditioned molecular generation for structured proteins. Guided by multi‐task binding‐site supervision, it aligns interaction‐critical residues before learning drug‐target representations and simultaneously infers ...
Luo G +6 more
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Sequence-encoded determinants drive distinct early aggregation pathways and different structural outcomes in PNT1 fibrils across Henipavirus members. [PDF]
Protein SciAbstract Protein aggregation is increasingly recognized as a biologically relevant process in viral proteins, yet the molecular determinants governing such phenomena remain poorly understood. Intrinsically disordered proteins (IDPs) are ubiquitous in viral proteomes, where conformational plasticity not only enables functional diversity but also permits
Sawdekar H +6 more
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Intrinsically disordered proteins studied by NMR spectroscopy
Journal of Magnetic Resonance OpenIntrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of complex multi-domain proteins are now identified as a trend topic by the scientific community.
Marco Schiavina +7 more
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idpr: A package for profiling and analyzing Intrinsically Disordered Proteins in R
PLoS ONE, 2022 Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are proteins or protein-domains that do not have a single native structure, rather, they are a class of flexible peptides that can rapidly adopt multiple conformations ...
William M. McFadden, Judith L. Yanowitz
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