Book ; Online: Frontiers in Protein Folding and Related Areas - in Memory of Professor Sir Christopher M. Dobson (1949-2019)
2023
Keywords | Research & information: general ; Biology, life sciences ; 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 |
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Language | English |
Size | 1 electronic resource (418 pages) |
Publisher | MDPI - Multidisciplinary Digital Publishing Institute |
Publishing place | Basel |
Document type | Book ; Online |
Note | English |
HBZ-ID | HT030376814 |
ISBN | 9783036573205 ; 3036573208 |
Database | ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture |
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