LEADER 06516nam 2201669z- 450 001 9910557509403321 005 20210501 035 $a(CKB)5400000000044462 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/68945 035 $a(oapen)doab68945 035 $a(EXLCZ)995400000000044462 100 $a20202105d2020 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$aFunctionally Relevant Macromolecular Interactions of Disordered Proteins 210 $aBasel, Switzerland$cMDPI - Multidisciplinary Digital Publishing Institute$d2020 215 $a1 online resource (520 p.) 311 08$a3-03936-521-5 311 08$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 $aBiology, life sciences$2bicssc 606 $aResearch and information: general$2bicssc 610 $aaggregation 610 $aCABS model 610 $aco-evolution 610 $acoarse-grained 610 $aconformational plasticity 610 $acopper binding 610 $acorrelated mutations 610 $adecision tree based artificial neural network 610 $adehydron 610 $adifferentially regulated genes 610 $adisorder-to-order regions 610 $adisordered protein 610 $adisordered protein platform 610 $aDNA conformational landscape 610 $aDNA-protein interactions 610 $adrug discovery 610 $adrugs 610 $adual threshold 610 $aeIF4E 610 $aepiproteome 610 $aevolution 610 $aevolutionary couplings 610 $aextracellular 610 $aFG-Nups 610 $afluorescence anisotropy 610 $afolding 610 $afunctional analysis 610 $agene ontology analysis 610 $ahistone lysine methyltransferase 610 $ahomodimer 610 $aHOTAIR 610 $ahydration 610 $ahydrogen bond 610 $aimmune 610 $ainter-subunit interaction 610 $ainteraction surface 610 $aintrinsic disorder 610 $aintrinsic disorder prediction 610 $aintrinsically disorder proteins 610 $aintrinsically disordered 610 $aintrinsically disordered protein 610 $aintrinsically disordered proteins 610 $aintrinsically disordered proteins (IDPs) 610 $aintrinsically disordered region 610 $aion pair 610 $aleukemia 610 $alncRNA 610 $aMC simulations 610 $aMEG3 610 $amembrane-less organelle 610 $ameta strategy 610 $aMicroarray 610 $aMLL proteins 610 $aMLL4 610 $amolecular machines 610 $amolecular recognition feature 610 $amolten globule 610 $amutual synergistic folding 610 $aN-terminal prion protein 610 $aneurodegenerative disease 610 $aneurodegenerative diseases 610 $aNuclear pore complex 610 $aoligomer 610 $ap300 HAT acetylation 610 $ap53 610 $aphosphorylation 610 $aphysiological homeostasis 610 $aplant virus 610 $apost-translational modification 610 $apost-translational modifications 610 $apotyvirus 610 $aprion disease mutations 610 $aprotein 610 $aprotein aggregation 610 $aprotein conformation 610 $aprotein hydrodynamics 610 $aprotein intrinsic disorder 610 $aprotein stability 610 $aprotein structure 610 $aprotein thermostability 610 $aprotein-protein interaction 610 $aprotein-RNA interactions 610 $aresidue co-variation 610 $aresidue contact network 610 $aribosomal protein 610 $aRIN4 610 $aRNA binding 610 $aRNA sequencing 610 $asalt bridges 610 $asecretion 610 $asequential DNA bending 610 $asignificance voting 610 $asmFRET 610 $asolvent-accessible surface area 610 $aSox2 sequential DNA loading 610 $aspectroscopy 610 $astabilization center 610 $astatistical force fields 610 $astress response 610 $astructural disorder 610 $astructural domain 610 $aTau fibrillation 610 $atemperature response 610 $atranscription factor dosage 610 $atranscription factors 610 $atranscriptome 610 $aunstructured proteins 610 $aVPg 610 $awide-line 1H NMR 615 7$aBiology, life sciences 615 7$aResearch and information: general 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