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Functionally Relevant Macromolecular Interactions of Disordered Proteins

Resumen/Descripción – provisto por la editorial

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Palabras clave – provistas por la editorial

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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Información

Tipo de recurso:

libros

ISBN electrónico

978-3-03936-522-7

País de edición

Suiza