Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019)

Contributors: Kuwajima, Kunihiro, Okamoto, Yuko, Knowles, Tuomas, Vendruscolo, Michele

Subject Terms: 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, Research and information: general, Biology, life sciences

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Access URL: https://directory.doabooks.org/handle/20.500.12854/100802
https://mdpi.com/books/pdfview/book/7265

The Structural Rule Distinguishing a Superfold: A Case Study of Ferredoxin Fold and the Reverse Ferredoxin Fold

Authors: Takumi Nishina, Megumi Nakajima, Masaki Sasai, George Chikenji

Source: Molecules, Vol 27, Iss 11, p 3547 (2022)

Subject Terms: protein design, reverse fold, minimum frustration, Organic chemistry, QD241-441

File Description: electronic resource

Relation: https://www.mdpi.com/1420-3049/27/11/3547; https://doaj.org/toc/1420-3049

Access URL: https://doaj.org/article/f643443fd078461bb025c5a23d864422

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