Reprint

Physics of Protein Folding, Misfolding, and Intrinsic Disorder: A Themed Issue in Honour of Professor Vladimir Uversky on the Occasion of His 60th Birthday

Edited by
October 2023
486 pages
  • ISBN978-3-0365-9112-4 (Hardback)
  • ISBN978-3-0365-9113-1 (PDF)

This book is a reprint of the Special Issue Physics of Protein Folding, Misfolding, and Intrinsic Disorder: A Themed Issue in Honour of Professor Vladimir Uversky on the Occasion of His 60th Birthday that was published in

Biology & Life Sciences
Medicine & Pharmacology
Summary

This Special Issue of Biomolecules, “Physics of Protein Folding, Misfolding, and Intrinsic Disorder: A Themed Issue in Honour of Professor Vladimir Uversky on the Occasion of His 60th Birthday”, is a dedication to one of the discoverers of IDPs. This collection is a small token of the respect, admiration, and affection the contributors have for Prof. Vladimir (Volodya) Uversky. It is also a celebration of his illustrious career, and his accomplishments, and contributions to the IDP field that have inspired so many minds worldwide. This Special Issue presents the state of the art as it emerges from the contribution of the community of IDP researchers (IDPers), who have responded to the invitation to give credit to the pioneering work of Prof. Vladimir Uversky aimed at defining the class of disordered proteins and at promoting the attention of scientists toward the existence of “non-globular proteins”. The papers in this collection show the advancement of our knowledge through the application of an integrative structural approach and witnesses at the same time the interest of the IDPer community toward new concepts (i.e., liquid-liquid phase separation) and new methodological frontiers (i.e., the application of machine learning and artificial intelligence to disorder prediction and modelling).

Format
  • Hardback
License
© 2022 by the authors; CC BY-NC-ND license
Keywords
charge clustering; polyelectrolytes; average shape of conformational ensembles; charged-residue patterning; hydrodynamic radius; solvent-accessible surface area; proline content; conformational compactness; ellipsoid model; intrinsically disordered proteins (IDPs); intrinsically disordered protein regions (IDRs); LC–MS/MS; IUPred analysis; Ostrinia nubilalis; cold hardiness; intrinsic disorder; intrinsically disordered proteins; intrinsic disordered regions; disorder scale; disorder propensity; amino acids; amino acid bias; predictive performance; disorder prediction; SARS-CoV-2; COVID-19; IDP; RNA; NMR; pH; liquid-liquid phase separation; intrinsically disordered proteins; protein solubility; protein disorder; mutations; bioinformatics; kinetics; fluorescence; site-directed mutagenesis; protein–protein interactions; SH2 domains; Crkl; Paxillin; Calvin-Benson-Bassham cycle; conditionally disordered protein; history of modern science; metabolism regulation; moonlighting protein; protein-protein interaction; biomolecular condensates; machine learning; predictor; physical interactions; intrinsically disordered proteins; phase separation; liquid–liquid phase separation; intrinsically disordered proteins; biomineralization; calcium carbonate; otoliths; nucleation pathways; nickel; intrinsically disordered regions; lung cancer; nmr; isothermal titration calorimetry; circular dichroism; light scattering; Dss1; intrinsically disordered protein; IDPs; molecular dynamics; NMR; sequence composition; SAXS; membrane-less organelles; intrinsically disordered proteins; liquid-liquid phase separation; stress; long foldable segments; pyHCA; soluble domains; protein sequence; conditional order; hidden order; dark proteomes; intrinsically disordered domains; phase separation; biomolecular condensates; coexistence line; tumor suppressor p53; intrinsically disordered proteins; intramolecular interaction; salt-dependent binding affinity; counterion condensation theory; DNA binding; fluorescence anisotropy; van’t Hoff; hydrodynamic radius; intrinsically disordered proteins (IDPs); protein purification; affinity chromatography; Tau; androgen receptor (AF1); isoform; large-scale analysis; protein structure; AlphaFold; canonical protein; alpha-synuclein; membrane; synaptic vesicle; synapsin; Parkinson’s; intrinsically disordered proteins; Myc; protein-protein interaction; drug targets; SLiM; small-molecule inhibitors; glutamate receptor; intrinsically disordered protein; discrete molecular dynamics; single molecule fluorescence; liquid-liquid phase separation; intrinsically disordered proteins; integrative structural biology; unfolded; unstructured; flexible; protein function; intrinsically disordered proteins; polymer physics; percolation; entanglement; RNA; topology; polymer rheology; biomolecular condensates; intrinsically disordered proteins; polyelectrolytes; D/E repeats; K/R repeats; molecular dynamics simulations; hub proteins; intrinsic disorder; multivalency; transcription factor; linker length; heterogeneity; dimers; duplexes; liquid–liquid phase separation; coarse-grained simulation; molecular mass; LLPS stability; FUS; n/a