Functionally Relevant Macromolecular Interactions of Disordered Proteins

• Otros Autores: Simon, Istvan (Editor)
• Formato: Electrónico Capítulo de libro
• Lenguaje: inglés
• Publicado: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2020
• Materias: 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
• Acceso en línea: DOAB: download the publication; DOAB: description of the publication

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...