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

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https://mdpi.com/books/pdfview/book/8061Contributor(s)
Kulkarni, Prakash (editor)
Brocca, Stefania (editor)
Dunker, Keith (editor)
Longhi, Sonia (editor)
Language
EnglishAbstract
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).
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; 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; phase separation; liquid–liquid phase separation; 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; sequence composition; SAXS; membrane-less organelles; stress; long foldable segments; pyHCA; soluble domains; protein sequence; conditional order; hidden order; dark proteomes; intrinsically disordered domains; coexistence line; tumor suppressor p53; intramolecular interaction; salt-dependent binding affinity; counterion condensation theory; DNA binding; fluorescence anisotropy; van’t Hoff; 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; Myc; drug targets; SLiM; small-molecule inhibitors; glutamate receptor; discrete molecular dynamics; single molecule fluorescence; integrative structural biology; unfolded; unstructured; flexible; protein function; polymer physics; percolation; entanglement; topology; polymer rheology; D/E repeats; K/R repeats; molecular dynamics simulations; hub proteins; multivalency; transcription factor; linker length; heterogeneity; dimers; duplexes; coarse-grained simulation; molecular mass; LLPS stability; FUS; n/aWebshop link
https://mdpi.com/books/pdfview ...ISBN
9783036591124, 9783036591131Publisher website
www.mdpi.com/booksPublication date and place
Basel, 2023Classification
Research and information: general
Biology, life sciences