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Palabras clave – provistas por la editorial

14-3-3 proteins; molecular chaperone; amyloid β; α-synuclein; NMR spectroscopy; amyloid fibril; amyloidogenesis; aggregation; adsorption; Aβ 1-40 peptide; boundary of liquid phase; self-assembly; extraction; solubilization; toxic oligomers; Parkinson’s disease; familial mutations; α-helical structure; amyloid-beta; mutants; cholesterol; simulations; X-ray crystallography; phospholipase A1; homodimer; dimerization domain; catalytic triad; plant protein; molecular dynamics simulation; replica permutation method; amyloid-β; disaggregation; β-sheet; α-helix; interface; inhibitor; polyphenol; high-temperature reversible oligomerization; amyloidogenicity; oligomeric interface residues; thermal denaturation; mutational analysis; RHIM; TRIF; necroptosis; functional amyloid; fibrils; RIPK; turbulent mixing; continuous flow; fluorescence; reaction mechanism; protein folding; protein–ligand interactions; protein design; reverse fold; minimum frustration; protein structure prediction; sequence-structure alignment; template-based modeling; conditional random fields; boosted regression trees; CASP; hydrogen/deuterium exchange; dimethylsulfoxide; nuclear magnetic resonance; chaperonin; GroEL; protease; Lon protease; proteomics; proteostasis; Hfq hexamer; mutations; unfolding intermediates; thermodynamics; amyloid; insulin B chain; nucleation; prefibrillar aggregates; protofibrils; bacterial amyloid; biofilm; curli; FapC; imperfect repeats; neurodegeneration; oligomerisation; native-like; micelle; globular protein; rigid native state; molten globule; intrinsically disordered; functional state; unfolded state; coil; post-translational modifications; membrane; chaperone; statistical mechanical model; WSME model; folding kinetics; folding intermediates; protein dynamics; amyloid fibrils; amorphous aggregation; β2-microglobulin; protein misfolding; solubility; supersaturation; ultrasonication; cryo-electron microscopy; fibril; ganglioside; cancer; prion; folding; pathway; interdiction; peptide; enhanced sampling method; molecular force fields; van der Waals interaction; CHARMM36m; NBFIX; intrinsically disordered proteins; crowding simulations