Three Functional States of Proteins

Three Functional States of Proteins

Structured, Intrinsically Disordered, and Phase Separated

Tripathi, Timir; Uversky, Vladimir N

Elsevier Science Publishing Co Inc

12/2024

474

Mole

9780443218095

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1. The three functional states of proteins: Beyond the classical "lock-and-key" paradigm
2. Ordered proteins and structure-function relationship: Classical view
3. Binding of a substrate ("lock and key") and conformational adaption ("induced fit") are different stages of enzyme action
4. Intrinsically disordered proteins: Functionality of chaos
5. Protein Conformation-based Phenotypic Switching and Implications in the Origin and Evolution of Multicellularity
6. Hybrid proteins: Fusion chimeras and natural wonders
7. Functional protein oligomers
8. Fuzzy complexes
9. SMARTQ: Single Molecule Amyloid fibRil Tracking and Quantification. A method for accurately imaging, tracking and quantifying the growth of individual amyloid fibrils using TIRF
10. Structural Polymorphism in Amyloids - States within Proteins' Solid-State
11. Liquid-Liquid Phase Separation, Biomolecular Condensates and Membraneless Organelles: A Novel Blueprint of Intracellular Organization
12. Physical principles and molecular interactions underlying protein phase separation
13. Various levels of phase transitions in the protein universe
14. Targeting phase-separated protein states for drug discovery
15. Protein hydrogels: Structure, Characteristics, and Applications
16. Interactions among the three protein states
17. Protein frustration and fuzziness in the three functional states
18. Thermoresponsive intrinsically disordered protein polymers
19. The evolution and exploration of intrinsically disordered and phase-separated protein states
20. Computational modelling of intrinsically disordered and phase separated protein states
21. Molecular dynamics simulations of intrinsically disordered, fuzzy complexes, and phase separated protein states
22. Biological complexity of the phase separated protein states
23. Protein structure-function continuum
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Adaptive evolution; Alzheimer's disease; Amyloid; Amyloid fibril; Amyloid fibrils; Analytical ultracentrifugation; Binding affinity; Binding mode multiplicity; Bioinformatics; Biomedical applications; Biomolecular condensate; Biomolecular condensates; Biomolecular condensates across the tree of life; Cell and drug delivery; Cell mechanobiology; Cellular processes; Chemical shift perturbation; Circadian circuit; Coarse-grained simulations; Coil; Collagen-like polypeptide; Conformational dynamics; Conformational ensemble; Conformational heterogeneity; Conformational selection; Cross-saturation; Crosslinking strategies; Crystallization; CsgA; De novo proteins; Disorder across the tree of life; Disordered regions; Elastin-like polypeptide; Energetic frustration; Energy landscapes; Engineered protein-based hydrogels; "All-or-none? transition; Enzyme oligomers; Evolutionary rates; Evolutionary transition; Fibrils; Folding funnel; Freezing; Functional oligomers; Fuzziness; Fuzzy complex; Fuzzy complexes; Fuzzy interactions; Glutamine-rich polypeptide; Hetero-oligomers; Heterogeneity; Heterotypic; Homo-oligomers; Homology detection; Hybrid proteins; Induced fit model; Interactions; Intracellular space; Intrinsic disorder; Intrinsically disordered protein; Intrinsically disordered protein regions; Intrinsically disordered proteins; Intrinsically disordered proteins/regions; Intrinsically disordered region; Intrinsically disordered regions; Levinthal's paradox; Ligand binding; Liquid-liquid phase separation; Liquid-liquid phase separation; Liquid-liquid transition; Lock and key model; Low complexity domains; Lower critical solution temperature; Machine learning; Membrane-bound organelles; Membrane-less organelle; Membrane-less organelles; Metabolic diseases; MoRFs; Molecular dynamics simulations; Molecular scavengers; Molten globule; Monte Carlo simulations; Multicellularity; Multivalent interactions; Natural-protein-based hydrogels; Neurodegenerative disorders; Nuclear magnetic resonance; Nucleation; Oligomer; Ordered proteins; Origin of life; Parkinson's disease; Peak broadening; Phase separation; Phase transition; Phase-separated protein states; Phenotypic switching; Polymorphism; Post-translational modifications