06516nam 2201669z- 450 991055750940332120210501(CKB)5400000000044462(oapen)https://directory.doabooks.org/handle/20.500.12854/68945(oapen)doab68945(EXLCZ)99540000000004446220202105d2020 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierFunctionally Relevant Macromolecular Interactions of Disordered ProteinsBasel, SwitzerlandMDPI - Multidisciplinary Digital Publishing Institute20201 online resource (520 p.)3-03936-521-5 3-03936-522-3 Disordered 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.Biology, life sciencesbicsscResearch and information: generalbicsscaggregationCABS modelco-evolutioncoarse-grainedconformational plasticitycopper bindingcorrelated mutationsdecision tree based artificial neural networkdehydrondifferentially regulated genesdisorder-to-order regionsdisordered proteindisordered protein platformDNA conformational landscapeDNA-protein interactionsdrug discoverydrugsdual thresholdeIF4Eepiproteomeevolutionevolutionary couplingsextracellularFG-Nupsfluorescence anisotropyfoldingfunctional analysisgene ontology analysishistone lysine methyltransferasehomodimerHOTAIRhydrationhydrogen bondimmuneinter-subunit interactioninteraction surfaceintrinsic disorderintrinsic disorder predictionintrinsically disorder proteinsintrinsically disorderedintrinsically disordered proteinintrinsically disordered proteinsintrinsically disordered proteins (IDPs)intrinsically disordered regionion pairleukemialncRNAMC simulationsMEG3membrane-less organellemeta strategyMicroarrayMLL proteinsMLL4molecular machinesmolecular recognition featuremolten globulemutual synergistic foldingN-terminal prion proteinneurodegenerative diseaseneurodegenerative diseasesNuclear pore complexoligomerp300 HAT acetylationp53phosphorylationphysiological homeostasisplant viruspost-translational modificationpost-translational modificationspotyvirusprion disease mutationsproteinprotein aggregationprotein conformationprotein hydrodynamicsprotein intrinsic disorderprotein stabilityprotein structureprotein thermostabilityprotein-protein interactionprotein-RNA interactionsresidue co-variationresidue contact networkribosomal proteinRIN4RNA bindingRNA sequencingsalt bridgessecretionsequential DNA bendingsignificance votingsmFRETsolvent-accessible surface areaSox2 sequential DNA loadingspectroscopystabilization centerstatistical force fieldsstress responsestructural disorderstructural domainTau fibrillationtemperature responsetranscription factor dosagetranscription factorstranscriptomeunstructured proteinsVPgwide-line 1H NMRBiology, life sciencesResearch and information: generalSimon Istvanedt685751Simon IstvanothBOOK9910557509403321Functionally Relevant Macromolecular Interactions of Disordered Proteins3021309UNINA