Results 1 to 10 of about 3,579,241 (217)

Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness [PDF]

Microbiologyopen
The 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, Ryan M, Hudson S, Thompson D.   +3 more
europepmc   +2 more sources

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, Zhang Q, Wang C, Yi Z, Wang AJ, Tang J, Li M.   +6 more
europepmc   +2 more sources

Prediction of protein-protein interaction sites in intrinsically disordered proteins

Frontiers in Molecular Biosciences, 2022
Intrinsically disordered proteins (IDPs) participate in many biological processes by interacting with other proteins, including the regulation of transcription, translation, and the cell cycle.
Ranran Chen, Ranran Chen, Xinlu Li, Xinlu Li, Yaqing Yang, Yaqing Yang, Xixi Song, Xixi Song, Cheng Wang, Cheng Wang, Dongdong Qiao   +10 more
doaj   +3 more sources

A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers. [PDF]

Adv Sci (Weinh)
Phase separation and aging of intrinsically disordered proteins are placed in a unifying framework. A thermodynamically consistent time‐dependent version of associating‐polymer theory shows how the processes are intricately coupled. Assuming aging to occur through interacting sites resulting from reversible conformational transitions, the model ...
Michels JJ, Caria J, Lemke EA.
europepmc   +2 more sources

Inherent α-Helix Around Tyrosine 183 in the Intrinsically Disordered Tail of the Multi-Site Docking Platform Gab1. [PDF]

Biopolymers
The two phosphorylation sites within the Gab1 fragment 142‐203 exhibit distinct structural characteristics. Tyr162 is in a disordered region, Y183 in a helical segment. ABSTRACT The biological function of intrinsically disordered proteins is frequently coupled to short linear motifs, which serve as protein binding sites.
Dietrich A, Lewitzky M, Gruber T, Balbach J, Feller SM, Weininger U.   +5 more
europepmc   +2 more sources

Conformational ensembles of the disordered 4E-BP2:eIF4E complex restrained by smFRET experiments. [PDF]

Protein Sci
Abstract Eukaryotic cap‐dependent translation initiation is regulated by binding of the predominantly folded eukaryotic initiation factor 4E (eIF4E) to the intrinsically disordered eIF4E binding proteins (4E‐BPs). Here, we report full‐length atomistic conformational ensembles generated by IDPConformerGenerator and optimized by X‐EISDv2 workflow for ...
Smyth S, Liu ZH, Tsangaris TE, Head-Gordon T, Forman-Kay JD, Gradinaru CC.   +5 more
europepmc   +2 more sources

Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins

Biomolecules, 2018
Intrinsically disordered proteins (IDPs) are often modeled using ideas from polymer physics that suggest they smoothly explore all corners of configuration space.
Sharonda J. LeBlanc, Prakash Kulkarni, Keith R. Weninger   +2 more
doaj   +3 more sources

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
doaj   +3 more sources

Prediction of folding patterns for intrinsic disordered protein

Scientific Reports, 2023
The conformation flexibility of natural protein causes both complexity and difficulty to understand the relationship between structure and function. The prediction of intrinsically disordered protein primarily is focusing on to disclose the regions with ...
Jiaan Yang, Wen-xiang Cheng, Gang Wu, Sitong Sheng, Peng Zhang   +4 more
doaj   +1 more source

Identification of ligand binding sites in intrinsically disordered proteins with a differential binding score

Scientific Reports, 2021
Screening ligands directly binding to an ensemble of intrinsically disordered proteins (IDP) to discover potential hits or leads for new drugs is an emerging but challenging area as IDPs lack well-defined and ordered 3D-protein structures.
Qiao-Hong Chen, V. V. Krishnan
doaj   +1 more source