LEADER 06503nam 2201657z- 450 001 9910557509403321 005 20231214133334.0 035 $a(CKB)5400000000044462 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/68945 035 $a(EXLCZ)995400000000044462 100 $a20202105d2020 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aFunctionally Relevant Macromolecular Interactions of Disordered Proteins 210 $aBasel, Switzerland$cMDPI - Multidisciplinary Digital Publishing Institute$d2020 215 $a1 electronic resource (520 p.) 311 $a3-03936-521-5 311 $a3-03936-522-3 330 $aDisordered proteins are relatively recent newcomers in protein science. They were first described in detail by Wright and Dyson, in their J. Mol. Biol. paper in 1999. First, it was generally thought for more than a decade that disordered proteins or disordered parts of proteins have different amino acid compositions than folded proteins, and various prediction methods were developed based on this principle. These methods were suitable for distinguishing between the disordered (unstructured) and structured proteins known at that time. In addition, they could predict the site where a folded protein binds to the disordered part of a protein, shaping the latter into a well-defined 3D structure. Recently, however, evidence has emerged for a new type of disordered protein family whose members can undergo coupled folding and binding without the involvement of any folded proteins. Instead, they interact with each other, stabilizing their structure via ?mutual synergistic folding? and, surprisingly, they exhibit the same residue composition as the folded protein. Increasingly more examples have been found where disordered proteins interact with non-protein macromolecules, adding to the already large variety of protein?protein interactions. There is also a very new phenomenon when proteins are involved in phase separation, which can represent a weak but functionally important macromolecular interaction. These phenomena are presented and discussed in the chapters of this book. 606 $aResearch & information: general$2bicssc 606 $aBiology, life sciences$2bicssc 610 $aintrinsically disordered proteins 610 $aepiproteome 610 $adisordered protein platform 610 $amolecular recognition feature 610 $apost-translational modifications 610 $aphysiological homeostasis 610 $astress response 610 $aRIN4 610 $ap53 610 $amolecular machines 610 $aintrinsically disordered protein 610 $amembrane-less organelle 610 $aneurodegenerative disease 610 $ap300 HAT acetylation 610 $apost-translational modification 610 $aprotein aggregation 610 $aTau fibrillation 610 $aintrinsically disorder proteins 610 $adisorder-to-order regions 610 $aprotein?RNA interactions 610 $aunstructured proteins 610 $aconformational plasticity 610 $adisordered protein 610 $afolding 610 $aribosomal protein 610 $aspectroscopy 610 $aprotein stability 610 $atemperature response 610 $aprotein thermostability 610 $asalt bridges 610 $ameta strategy 610 $adual threshold 610 $asignificance voting 610 $adecision tree based artificial neural network 610 $aprotein intrinsic disorder 610 $aintrinsic disorder 610 $aintrinsic disorder prediction 610 $aintrinsically disordered region 610 $aprotein conformation 610 $atranscriptome 610 $aRNA sequencing 610 $aMicroarray 610 $adifferentially regulated genes 610 $agene ontology analysis 610 $afunctional analysis 610 $aintrinsically disordered 610 $astructural disorder 610 $acorrelated mutations 610 $aco-evolution 610 $aevolutionary couplings 610 $aresidue co-variation 610 $ainteraction surface 610 $aresidue contact network 610 $adehydron 610 $ahomodimer 610 $ahydrogen bond 610 $ainter-subunit interaction 610 $aion pair 610 $amutual synergistic folding 610 $asolvent-accessible surface area 610 $astabilization center 610 $aMLL proteins 610 $aMLL4 610 $alncRNA 610 $aHOTAIR 610 $aMEG3 610 $aleukemia 610 $ahistone lysine methyltransferase 610 $aRNA binding 610 $aprotein 610 $ahydration 610 $awide-line 1H NMR 610 $asecretion 610 $aimmune 610 $aextracellular 610 $aprotein-protein interaction 610 $astructural domain 610 $aevolution 610 $atranscription factors 610 $aDNA-protein interactions 610 $aSox2 sequential DNA loading 610 $asmFRET 610 $aDNA conformational landscape 610 $asequential DNA bending 610 $atranscription factor dosage 610 $aoligomer 610 $aN-terminal prion protein 610 $acopper binding 610 $aprion disease mutations 610 $aNuclear pore complex 610 $aFG-Nups 610 $aphosphorylation 610 $acoarse-grained 610 $aCABS model 610 $aMC simulations 610 $astatistical force fields 610 $aprotein structure 610 $aintrinsically disordered proteins (IDPs) 610 $aneurodegenerative diseases 610 $aaggregation 610 $adrugs 610 $adrug discovery 610 $aplant virus 610 $aeIF4E 610 $aVPg 610 $apotyvirus 610 $amolten globule 610 $afluorescence anisotropy 610 $aprotein hydrodynamics 615 7$aResearch & information: general 615 7$aBiology, life sciences 700 $aSimon$b Istvan$4edt$0685751 702 $aSimon$b Istvan$4oth 906 $aBOOK 912 $a9910557509403321 996 $aFunctionally Relevant Macromolecular Interactions of Disordered Proteins$93021309 997 $aUNINA