Reprint
Functionally Relevant Macromolecular Interactions of Disordered Proteins
Edited by
August 2020
520 pages
- ISBN978-3-03936-521-0 (Hardback)
- ISBN978-3-03936-522-7 (PDF)
This book is a reprint of the Special Issue Functionally Relevant Macromolecular Interactions of Disordered Proteins that was published in
Biology & Life Sciences
Chemistry & Materials Science
Medicine & Pharmacology
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.
Format
- Hardback
License
© 2020 by the authors; CC BY-NC-ND license
Keywords
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; intrinsically disordered proteins; 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; disordered protein; structural disorder; correlated mutations; co-evolution; evolutionary couplings; residue co-variation; interaction surface; residue contact network; dehydron; homodimer; hydrogen bond; inter-subunit interaction; intrinsically disordered protein; ion pair; mutual synergistic folding; solvent-accessible surface area; stabilization center; MLL proteins; MLL4; lncRNA; HOTAIR; MEG3; leukemia; histone lysine methyltransferase; RNA binding; intrinsically disordered protein; protein; hydration; wide-line 1H NMR; secretion; immune; extracellular; protein-protein interaction; intrinsically disordered region; structural domain; evolution; transcription factors; DNA-protein interactions; Sox2 sequential DNA loading; smFRET; DNA conformational landscape; sequential DNA bending; transcription factor dosage; disordered protein; folding; oligomer; ribosomal protein; protein stability; N-terminal prion protein; copper binding; prion disease mutations; Nuclear pore complex; FG-Nups; phosphorylation; coarse-grained; CABS model; MC simulations; statistical force fields; disordered protein; protein structure; intrinsically disordered proteins (IDPs); neurodegenerative diseases; aggregation; drugs; drug discovery; intrinsically disordered protein; plant virus; eIF4E; VPg; potyvirus; molten globule; protein-protein interaction; fluorescence anisotropy; protein hydrodynamics