06503nam 2201657z- 450 991055750940332120231214133334.0(CKB)5400000000044462(oapen)https://directory.doabooks.org/handle/20.500.12854/68945(EXLCZ)99540000000004446220202105d2020 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierFunctionally Relevant Macromolecular Interactions of Disordered ProteinsBasel, SwitzerlandMDPI - Multidisciplinary Digital Publishing Institute20201 electronic 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.Research & information: generalbicsscBiology, life sciencesbicsscintrinsically disordered proteinsepiproteomedisordered protein platformmolecular recognition featurepost-translational modificationsphysiological homeostasisstress responseRIN4p53molecular machinesintrinsically disordered proteinmembrane-less organelleneurodegenerative diseasep300 HAT acetylationpost-translational modificationprotein aggregationTau fibrillationintrinsically disorder proteinsdisorder-to-order regionsprotein–RNA interactionsunstructured proteinsconformational plasticitydisordered proteinfoldingribosomal proteinspectroscopyprotein stabilitytemperature responseprotein thermostabilitysalt bridgesmeta strategydual thresholdsignificance votingdecision tree based artificial neural networkprotein intrinsic disorderintrinsic disorderintrinsic disorder predictionintrinsically disordered regionprotein conformationtranscriptomeRNA sequencingMicroarraydifferentially regulated genesgene ontology analysisfunctional analysisintrinsically disorderedstructural disordercorrelated mutationsco-evolutionevolutionary couplingsresidue co-variationinteraction surfaceresidue contact networkdehydronhomodimerhydrogen bondinter-subunit interactionion pairmutual synergistic foldingsolvent-accessible surface areastabilization centerMLL proteinsMLL4lncRNAHOTAIRMEG3leukemiahistone lysine methyltransferaseRNA bindingproteinhydrationwide-line 1H NMRsecretionimmuneextracellularprotein-protein interactionstructural domainevolutiontranscription factorsDNA-protein interactionsSox2 sequential DNA loadingsmFRETDNA conformational landscapesequential DNA bendingtranscription factor dosageoligomerN-terminal prion proteincopper bindingprion disease mutationsNuclear pore complexFG-Nupsphosphorylationcoarse-grainedCABS modelMC simulationsstatistical force fieldsprotein structureintrinsically disordered proteins (IDPs)neurodegenerative diseasesaggregationdrugsdrug discoveryplant viruseIF4EVPgpotyvirusmolten globulefluorescence anisotropyprotein hydrodynamicsResearch & information: generalBiology, life sciencesSimon Istvanedt685751Simon IstvanothBOOK9910557509403321Functionally Relevant Macromolecular Interactions of Disordered Proteins3021309UNINA