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1. Intrinsically disordered proteins studied by NMR spectroscopy
by Felli, Isabella C., editor and Pierattelli, Roberta, editor
2015, 1st ed. 2015, Advances in experimental medicine and biology, ISBN 9783319201634, Volume 870, xiii, 421
This book discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional... 
Proteins | methods | Intrinsically Disordered Proteins | Nuclear Magnetic Resonance, Biomolecular | Nuclear magnetic resonance spectroscopy | Protein Conformation | Spectra | analysis | Protein Folding | Cytology | Life Sciences | Protein Science | Bioinformatics | Cell Biology
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2. Full Text Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
by Oldfield, Christopher J and Dunker, A. Keith
Annual Review of Biochemistry, ISSN 0066-4154, 6/2014, Volume 83, Issue 1, pp. 553 - 584
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and... 
chameleon | flexible | malleable | unstructured | rheomorphic | natively | inherently | unfolded | UNSTRUCTURED PROTEINS | MOLECULAR RECOGNITION FEATURES | MOLTEN GLOBULE STATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CALCIUM-PHOSPHATE NANOCLUSTERS | CONDITIONAL DISORDER | AMINO-ACID-SEQUENCE | FUNCTIONAL ANTHOLOGY | IN-CELL NMR | STRUCTURAL DISORDER | C-TERMINAL DOMAIN | Protein Structure, Tertiary | Electron Spin Resonance Spectroscopy | Magnetic Resonance Spectroscopy | Protein Structure, Secondary | Humans | Calcineurin - chemistry | Computational Biology | Solubility | Models, Molecular | Fibrinogen - chemistry | Trypsinogen - chemistry | Protein Interaction Mapping | Fibrin - chemistry | Animals | Caseins - chemistry | Intrinsically Disordered Proteins - chemistry | X-Ray Diffraction | Protein Binding | Scattering, Radiation | Phosvitin - chemistry | Trypsin - chemistry | Physiological aspects | Protein research | Research | Protein-protein interactions | Membrane proteins
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3. Full Text Modulation of intrinsically disordered protein function by post-translational modifications
by Bah, Alaji and Forman-Kay, Julie D
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 6696 - 6705
Post-translational modifications (PTMs) produce significant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting their... 
post-translational modification (PTM) | UNSTRUCTURED PROTEINS | intrinsically disordered protein | PHASE-TRANSITIONS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | protein-DNA interaction | MULTISITE PHOSPHORYLATION | protein conformation | TRANSLATION INITIATION | ETS-1 DNA-BINDING | GAMMA-CARBOXYGLUTAMIC ACID | regulation | MOLECULAR RECOGNITION | STRUCTURAL DISORDER | protein-protein interaction | INTERMOLECULAR INTERACTIONS | Eukaryotic Initiation Factors - chemistry | Eukaryotic Initiation Factors - genetics | Eukaryotic Initiation Factors - metabolism | Factor IX - chemistry | Chromatin | Phosphorylation | Protein Structure, Secondary | Humans | Amino Acids - chemistry | Factor IX - genetics | Static Electricity | Intrinsically Disordered Proteins - genetics | Protein Folding | Amino Acids - metabolism | Thermodynamics | Intrinsically Disordered Proteins - chemistry | Histones | Hydrophobic and Hydrophilic Interactions | Protein Binding | Factor IX - metabolism | Protein Interaction Domains and Motifs | Protein Processing, Post-Translational | Intrinsically Disordered Proteins - metabolism | Minireviews
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4. Full Text Intrinsically disordered proteins from A to Z
by Uversky, Vladimir N
International Journal of Biochemistry and Cell Biology, ISSN 1357-2725, 2011, Volume 43, Issue 8, pp. 1090 - 1103
The ideas that proteins might possess specific functions without being uniquely folded into rigid 3D-structures and that these floppy polypeptides might... 
Protein non-folding | Intrinsically disordered proteins | Protein structure | Protein function | Protein–protein interaction | Protein-protein interaction | UNSTRUCTURED PROTEINS | MOLECULAR RECOGNITION FEATURES | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHAMELEON SEQUENCES | CELL BIOLOGY | NATIVELY UNFOLDED PROTEINS | FUNCTIONAL ANTHOLOGY | STRUCTURAL DISORDER | HUMAN GENETIC-DISEASES | SECONDARY STRUCTURE | INTERACTION NETWORKS | FLY-CASTING MECHANISM | Protein Structure, Tertiary | Proteins - metabolism | Humans | Computational Biology | Protein Conformation | Protein Processing, Post-Translational | Structure-Activity Relationship | Proteins - chemistry | Protein Folding | Fuzzy logic | Proteins | Disorders | Biochemistry | Biology | Fuzzy set theory | Fuzzy | Fuzzy systems
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5. Full Text Intrinsically disordered proteins in cellular signalling and regulation
by Wright, Peter E and Wright, Peter E and Dyson, H. Jane
Nature reviews. Molecular cell biology, ISSN 1471-0072, 01/2015, Volume 16, Issue 1, pp. 18 - 29
Intrinsically disordered proteins (IDPs) are important components of the cellular signalling machinery, allowing the same polypeptide to undertake different... 
UNSTRUCTURED PROTEINS | TERMINAL DOMAIN | STRUCTURAL DISORDER | KIX DOMAIN | MULTISITE PHOSPHORYLATION | PEPTIDE MOTIFS | ADENOVIRUS E1A | TRANSACTIVATION DOMAIN | BINDING | WEB SERVER | CELL BIOLOGY | Multiprotein Complexes - metabolism | Animals | Humans | Alternative Splicing - physiology | Multiprotein Complexes - genetics | Signal Transduction - physiology | Intrinsically Disordered Proteins - genetics | Protein Processing, Post-Translational - physiology | Intrinsically Disordered Proteins - metabolism | Organ Specificity - physiology
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