TY - BOOK ID - 145541314 TI - Functionally Relevant Macromolecular Interactions of Disordered Proteins PY - 2020 PB - Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute DB - UniCat KW - Research & information: general KW - Biology, life sciences KW - intrinsically disordered proteins KW - epiproteome KW - disordered protein platform KW - molecular recognition feature KW - post-translational modifications KW - physiological homeostasis KW - stress response KW - RIN4 KW - p53 KW - molecular machines KW - intrinsically disordered protein KW - membrane-less organelle KW - neurodegenerative disease KW - p300 HAT acetylation KW - post-translational modification KW - protein aggregation KW - Tau fibrillation KW - intrinsically disorder proteins KW - disorder-to-order regions KW - protein–RNA interactions KW - unstructured proteins KW - conformational plasticity KW - disordered protein KW - folding KW - ribosomal protein KW - spectroscopy KW - protein stability KW - temperature response KW - protein thermostability KW - salt bridges KW - meta strategy KW - dual threshold KW - significance voting KW - decision tree based artificial neural network KW - protein intrinsic disorder KW - intrinsic disorder KW - intrinsic disorder prediction KW - intrinsically disordered region KW - protein conformation KW - transcriptome KW - RNA sequencing KW - Microarray KW - differentially regulated genes KW - gene ontology analysis KW - functional analysis KW - intrinsically disordered KW - structural disorder KW - correlated mutations KW - co-evolution KW - evolutionary couplings KW - residue co-variation KW - interaction surface KW - residue contact network KW - dehydron KW - homodimer KW - hydrogen bond KW - inter-subunit interaction KW - ion pair KW - mutual synergistic folding KW - solvent-accessible surface area KW - stabilization center KW - MLL proteins KW - MLL4 KW - lncRNA KW - HOTAIR KW - MEG3 KW - leukemia KW - histone lysine methyltransferase KW - RNA binding KW - protein KW - hydration KW - wide-line 1H NMR KW - secretion KW - immune KW - extracellular KW - protein-protein interaction KW - structural domain KW - evolution KW - transcription factors KW - DNA-protein interactions KW - Sox2 sequential DNA loading KW - smFRET KW - DNA conformational landscape KW - sequential DNA bending KW - transcription factor dosage KW - oligomer KW - N-terminal prion protein KW - copper binding KW - prion disease mutations KW - Nuclear pore complex KW - FG-Nups KW - phosphorylation KW - coarse-grained KW - CABS model KW - MC simulations KW - statistical force fields KW - protein structure KW - intrinsically disordered proteins (IDPs) KW - neurodegenerative diseases KW - aggregation KW - drugs KW - drug discovery KW - plant virus KW - eIF4E KW - VPg KW - potyvirus KW - molten globule KW - fluorescence anisotropy KW - protein hydrodynamics KW - intrinsically disordered proteins KW - epiproteome KW - disordered protein platform KW - molecular recognition feature KW - post-translational modifications KW - physiological homeostasis KW - stress response KW - RIN4 KW - p53 KW - molecular machines KW - intrinsically disordered protein KW - membrane-less organelle KW - neurodegenerative disease KW - p300 HAT acetylation KW - post-translational modification KW - protein aggregation KW - Tau fibrillation KW - intrinsically disorder proteins KW - disorder-to-order regions KW - protein–RNA interactions KW - unstructured proteins KW - conformational plasticity KW - disordered protein KW - folding KW - ribosomal protein KW - spectroscopy KW - protein stability KW - temperature response KW - protein thermostability KW - salt bridges KW - meta strategy KW - dual threshold KW - significance voting KW - decision tree based artificial neural network KW - protein intrinsic disorder KW - intrinsic disorder KW - intrinsic disorder prediction KW - intrinsically disordered region KW - protein conformation KW - transcriptome KW - RNA sequencing KW - Microarray KW - differentially regulated genes KW - gene ontology analysis KW - functional analysis KW - intrinsically disordered KW - structural disorder KW - correlated mutations KW - co-evolution KW - evolutionary couplings KW - residue co-variation KW - interaction surface KW - residue contact network KW - dehydron KW - homodimer KW - hydrogen bond KW - inter-subunit interaction KW - ion pair KW - mutual synergistic folding KW - solvent-accessible surface area KW - stabilization center KW - MLL proteins KW - MLL4 KW - lncRNA KW - HOTAIR KW - MEG3 KW - leukemia KW - histone lysine methyltransferase KW - RNA binding KW - protein KW - hydration KW - wide-line 1H NMR KW - secretion KW - immune KW - extracellular KW - protein-protein interaction KW - structural domain KW - evolution KW - transcription factors KW - DNA-protein interactions KW - Sox2 sequential DNA loading KW - smFRET KW - DNA conformational landscape KW - sequential DNA bending KW - transcription factor dosage KW - oligomer KW - N-terminal prion protein KW - copper binding KW - prion disease mutations KW - Nuclear pore complex KW - FG-Nups KW - phosphorylation KW - coarse-grained KW - CABS model KW - MC simulations KW - statistical force fields KW - protein structure KW - intrinsically disordered proteins (IDPs) KW - neurodegenerative diseases KW - aggregation KW - drugs KW - drug discovery KW - plant virus KW - eIF4E KW - VPg KW - potyvirus KW - molten globule KW - fluorescence anisotropy KW - protein hydrodynamics UR - https://www.unicat.be/uniCat?func=search&query=sysid:145541314 AB - 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. ER -