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Functionally Relevant Macromolecular Interactions of Disordered Proteins
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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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Keywords
- aggregation
- Biology, Life Sciences
- CABS model
- Co-Evolution
- coarse-grained
- conformational plasticity
- copper binding
- correlated mutations
- decision tree based artificial neural network
- dehydron
- differentially regulated genes
- disorder-to-order regions
- disordered protein
- disordered protein platform
- DNA conformational landscape
- DNA-protein interactions
- Drug Discovery
- Drugs
- dual threshold
- eIF4E
- epiproteome
- Evolution
- evolutionary couplings
- extracellular
- FG-Nups
- fluorescence anisotropy
- folding
- Functional analysis
- gene ontology analysis
- histone lysine methyltransferase
- homodimer
- HOTAIR
- hydration
- Hydrogen bond
- immune
- inter-subunit interaction
- interaction surface
- intrinsic disorder
- intrinsic disorder prediction
- intrinsically disorder proteins
- intrinsically disordered
- intrinsically disordered protein
- intrinsically disordered proteins
- intrinsically disordered proteins (IDPs)
- intrinsically disordered region
- ion pair
- Leukemia
- lncRNA
- Mathematics & science
- MC simulations
- MEG3
- membrane-less organelle
- meta strategy
- microarray
- MLL proteins
- MLL4
- molecular machines
- molecular recognition feature
- molten globule
- mutual synergistic folding
- N-terminal prion protein
- neurodegenerative disease
- Neurodegenerative Diseases
- nuclear pore complex
- oligomer
- p300 HAT acetylation
- p53
- Phosphorylation
- physiological homeostasis
- plant virus
- Post-translational modification
- post-translational modifications
- potyvirus
- prion disease mutations
- Protein
- protein aggregation
- Protein Conformation
- protein hydrodynamics
- protein intrinsic disorder
- protein stability
- protein structure
- protein thermostability
- protein-protein interaction
- protein–RNA interactions
- Reference, information & interdisciplinary subjects
- Research & information: general
- residue co-variation
- residue contact network
- ribosomal protein
- RIN4
- RNA binding
- RNA sequencing
- salt bridges
- secretion
- sequential DNA bending
- significance voting
- smFRET
- solvent-accessible surface area
- Sox2 sequential DNA loading
- spectroscopy
- stabilization center
- statistical force fields
- stress response
- structural disorder
- structural domain
- Tau fibrillation
- temperature response
- transcription factor dosage
- Transcription Factors
- transcriptome
- unstructured proteins
- VPg
- wide-line 1H NMR
Links
DOI: 10.3390/books978-3-03936-522-7Editions