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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Bibliographic Details
Other Authors:	Simon, Istvan (Editor)
Format:	Book Chapter
Published:	Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2020
Subjects:	Research & information: general Biology, life sciences intrinsically disordered proteins epiproteome disordered protein platform molecular recognition feature post-translational modifications physiological homeostasis stress response RIN4 p53 molecular machines intrinsically disordered protein membrane-less organelle neurodegenerative disease p300 HAT acetylation post-translational modification protein aggregation Tau fibrillation intrinsically disorder proteins disorder-to-order regions protein-RNA interactions unstructured proteins conformational plasticity disordered protein folding ribosomal protein spectroscopy protein stability temperature response protein thermostability salt bridges meta strategy dual threshold significance voting decision tree based artificial neural network protein intrinsic disorder intrinsic disorder intrinsic disorder prediction intrinsically disordered region protein conformation transcriptome RNA sequencing Microarray differentially regulated genes gene ontology analysis functional analysis intrinsically disordered structural disorder correlated mutations co-evolution evolutionary couplings residue co-variation interaction surface residue contact network dehydron homodimer hydrogen bond inter-subunit interaction ion pair mutual synergistic folding solvent-accessible surface area stabilization center MLL proteins MLL4 lncRNA HOTAIR MEG3 leukemia histone lysine methyltransferase RNA binding protein hydration wide-line 1H NMR secretion immune extracellular protein-protein interaction structural domain evolution transcription factors DNA-protein interactions Sox2 sequential DNA loading smFRET DNA conformational landscape sequential DNA bending transcription factor dosage oligomer N-terminal prion protein copper binding prion disease mutations Nuclear pore complex FG-Nups phosphorylation coarse-grained CABS model MC simulations statistical force fields protein structure intrinsically disordered proteins (IDPs) neurodegenerative diseases aggregation drugs drug discovery plant virus eIF4E VPg potyvirus molten globule fluorescence anisotropy protein hydrodynamics
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Summary:	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.
Physical Description:	1 electronic resource (520 p.)
ISBN:	books978-3-03936-522-7 9783039365210 9783039365227
Access:	Open Access

Functionally Relevant Macromolecular Interactions of Disordered Proteins

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