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dc.contributor.editorKulkarni, Prakash
dc.contributor.editorBrocca, Stefania
dc.contributor.editorDunker, Keith
dc.contributor.editorLonghi, Sonia
dc.date.accessioned2023-11-30T20:36:01Z
dc.date.available2023-11-30T20:36:01Z
dc.date.issued2023
dc.identifierONIX_20231130_9783036591124_61
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/128609
dc.description.abstractThis 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).
dc.languageEnglish
dc.subject.classificationthema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: generalen_US
dc.subject.classificationthema EDItEUR::P Mathematics and Science::PS Biology, life sciencesen_US
dc.subject.othercharge clustering
dc.subject.otherpolyelectrolytes
dc.subject.otheraverage shape of conformational ensembles
dc.subject.othercharged-residue patterning
dc.subject.otherhydrodynamic radius
dc.subject.othersolvent-accessible surface area
dc.subject.otherproline content
dc.subject.otherconformational compactness
dc.subject.otherellipsoid model
dc.subject.otherintrinsically disordered proteins (IDPs)
dc.subject.otherintrinsically disordered protein regions (IDRs)
dc.subject.otherLC–MS/MS
dc.subject.otherIUPred analysis
dc.subject.otherOstrinia nubilalis
dc.subject.othercold hardiness
dc.subject.otherintrinsic disorder
dc.subject.otherintrinsically disordered proteins
dc.subject.otherintrinsic disordered regions
dc.subject.otherdisorder scale
dc.subject.otherdisorder propensity
dc.subject.otheramino acids
dc.subject.otheramino acid bias
dc.subject.otherpredictive performance
dc.subject.otherdisorder prediction
dc.subject.otherSARS-CoV-2
dc.subject.otherCOVID-19
dc.subject.otherIDP
dc.subject.otherRNA
dc.subject.otherNMR
dc.subject.otherpH
dc.subject.otherliquid-liquid phase separation
dc.subject.otherprotein solubility
dc.subject.otherprotein disorder
dc.subject.othermutations
dc.subject.otherbioinformatics
dc.subject.otherkinetics
dc.subject.otherfluorescence
dc.subject.othersite-directed mutagenesis
dc.subject.otherprotein–protein interactions
dc.subject.otherSH2 domains
dc.subject.otherCrkl
dc.subject.otherPaxillin
dc.subject.otherCalvin-Benson-Bassham cycle
dc.subject.otherconditionally disordered protein
dc.subject.otherhistory of modern science
dc.subject.othermetabolism regulation
dc.subject.othermoonlighting protein
dc.subject.otherprotein-protein interaction
dc.subject.otherbiomolecular condensates
dc.subject.othermachine learning
dc.subject.otherpredictor
dc.subject.otherphysical interactions
dc.subject.otherphase separation
dc.subject.otherliquid–liquid phase separation
dc.subject.otherbiomineralization
dc.subject.othercalcium carbonate
dc.subject.otherotoliths
dc.subject.othernucleation pathways
dc.subject.othernickel
dc.subject.otherintrinsically disordered regions
dc.subject.otherlung cancer
dc.subject.othernmr
dc.subject.otherisothermal titration calorimetry
dc.subject.othercircular dichroism
dc.subject.otherlight scattering
dc.subject.otherDss1
dc.subject.otherintrinsically disordered protein
dc.subject.otherIDPs
dc.subject.othermolecular dynamics
dc.subject.othersequence composition
dc.subject.otherSAXS
dc.subject.othermembrane-less organelles
dc.subject.otherstress
dc.subject.otherlong foldable segments
dc.subject.otherpyHCA
dc.subject.othersoluble domains
dc.subject.otherprotein sequence
dc.subject.otherconditional order
dc.subject.otherhidden order
dc.subject.otherdark proteomes
dc.subject.otherintrinsically disordered domains
dc.subject.othercoexistence line
dc.subject.othertumor suppressor p53
dc.subject.otherintramolecular interaction
dc.subject.othersalt-dependent binding affinity
dc.subject.othercounterion condensation theory
dc.subject.otherDNA binding
dc.subject.otherfluorescence anisotropy
dc.subject.othervan’t Hoff
dc.subject.otherprotein purification
dc.subject.otheraffinity chromatography
dc.subject.otherTau
dc.subject.otherandrogen receptor (AF1)
dc.subject.otherisoform
dc.subject.otherlarge-scale analysis
dc.subject.otherprotein structure
dc.subject.otherAlphaFold
dc.subject.othercanonical protein
dc.subject.otheralpha-synuclein
dc.subject.othermembrane
dc.subject.othersynaptic vesicle
dc.subject.othersynapsin
dc.subject.otherParkinson’s
dc.subject.otherMyc
dc.subject.otherdrug targets
dc.subject.otherSLiM
dc.subject.othersmall-molecule inhibitors
dc.subject.otherglutamate receptor
dc.subject.otherdiscrete molecular dynamics
dc.subject.othersingle molecule fluorescence
dc.subject.otherintegrative structural biology
dc.subject.otherunfolded
dc.subject.otherunstructured
dc.subject.otherflexible
dc.subject.otherprotein function
dc.subject.otherpolymer physics
dc.subject.otherpercolation
dc.subject.otherentanglement
dc.subject.othertopology
dc.subject.otherpolymer rheology
dc.subject.otherD/E repeats
dc.subject.otherK/R repeats
dc.subject.othermolecular dynamics simulations
dc.subject.otherhub proteins
dc.subject.othermultivalency
dc.subject.othertranscription factor
dc.subject.otherlinker length
dc.subject.otherheterogeneity
dc.subject.otherdimers
dc.subject.otherduplexes
dc.subject.othercoarse-grained simulation
dc.subject.othermolecular mass
dc.subject.otherLLPS stability
dc.subject.otherFUS
dc.subject.othern/a
dc.titlePhysics of Protein Folding, Misfolding, and Intrinsic Disorder: A Themed Issue in Honour of Professor Vladimir Uversky on the Occasion of His 60th Birthday
dc.typebook
oapen.identifier.doi10.3390/books978-3-0365-9113-1
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn9783036591124
oapen.relation.isbn9783036591131
oapen.pages486
oapen.place.publicationBasel


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