Functionally Relevant Macromolecular Interactions of Disordered Proteins

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...

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Other Authors: Simon, Istvan (Editor)
Format: Book Chapter
Published: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2020
Subjects:
p53
VPg
Online Access:Get Fullteks
DOAB: description of the publication
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245 1 0 |a Functionally Relevant Macromolecular Interactions of Disordered Proteins 
260 |a Basel, Switzerland  |b MDPI - Multidisciplinary Digital Publishing Institute  |c 2020 
300 |a 1 electronic resource (520 p.) 
506 0 |a Open Access  |2 star  |f Unrestricted online access 
520 |a 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. 
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546 |a English 
650 7 |a Research & information: general  |2 bicssc 
650 7 |a Biology, life sciences  |2 bicssc 
653 |a intrinsically disordered proteins 
653 |a epiproteome 
653 |a disordered protein platform 
653 |a molecular recognition feature 
653 |a post-translational modifications 
653 |a physiological homeostasis 
653 |a stress response 
653 |a RIN4 
653 |a p53 
653 |a molecular machines 
653 |a intrinsically disordered protein 
653 |a membrane-less organelle 
653 |a neurodegenerative disease 
653 |a p300 HAT acetylation 
653 |a post-translational modification 
653 |a protein aggregation 
653 |a Tau fibrillation 
653 |a intrinsically disorder proteins 
653 |a disorder-to-order regions 
653 |a protein-RNA interactions 
653 |a unstructured proteins 
653 |a conformational plasticity 
653 |a disordered protein 
653 |a folding 
653 |a ribosomal protein 
653 |a spectroscopy 
653 |a protein stability 
653 |a temperature response 
653 |a protein thermostability 
653 |a salt bridges 
653 |a meta strategy 
653 |a dual threshold 
653 |a significance voting 
653 |a decision tree based artificial neural network 
653 |a protein intrinsic disorder 
653 |a intrinsic disorder 
653 |a intrinsic disorder prediction 
653 |a intrinsically disordered region 
653 |a protein conformation 
653 |a transcriptome 
653 |a RNA sequencing 
653 |a Microarray 
653 |a differentially regulated genes 
653 |a gene ontology analysis 
653 |a functional analysis 
653 |a intrinsically disordered 
653 |a structural disorder 
653 |a correlated mutations 
653 |a co-evolution 
653 |a evolutionary couplings 
653 |a residue co-variation 
653 |a interaction surface 
653 |a residue contact network 
653 |a dehydron 
653 |a homodimer 
653 |a hydrogen bond 
653 |a inter-subunit interaction 
653 |a ion pair 
653 |a mutual synergistic folding 
653 |a solvent-accessible surface area 
653 |a stabilization center 
653 |a MLL proteins 
653 |a MLL4 
653 |a lncRNA 
653 |a HOTAIR 
653 |a MEG3 
653 |a leukemia 
653 |a histone lysine methyltransferase 
653 |a RNA binding 
653 |a protein 
653 |a hydration 
653 |a wide-line 1H NMR 
653 |a secretion 
653 |a immune 
653 |a extracellular 
653 |a protein-protein interaction 
653 |a structural domain 
653 |a evolution 
653 |a transcription factors 
653 |a DNA-protein interactions 
653 |a Sox2 sequential DNA loading 
653 |a smFRET 
653 |a DNA conformational landscape 
653 |a sequential DNA bending 
653 |a transcription factor dosage 
653 |a oligomer 
653 |a N-terminal prion protein 
653 |a copper binding 
653 |a prion disease mutations 
653 |a Nuclear pore complex 
653 |a FG-Nups 
653 |a phosphorylation 
653 |a coarse-grained 
653 |a CABS model 
653 |a MC simulations 
653 |a statistical force fields 
653 |a protein structure 
653 |a intrinsically disordered proteins (IDPs) 
653 |a neurodegenerative diseases 
653 |a aggregation 
653 |a drugs 
653 |a drug discovery 
653 |a plant virus 
653 |a eIF4E 
653 |a VPg 
653 |a potyvirus 
653 |a molten globule 
653 |a fluorescence anisotropy 
653 |a protein hydrodynamics 
856 4 0 |a www.oapen.org  |u https://mdpi.com/books/pdfview/book/2712  |7 0  |z Get Fullteks 
856 4 0 |a www.oapen.org  |u https://directory.doabooks.org/handle/20.500.12854/68945  |7 0  |z DOAB: description of the publication