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

doi:10.3390/books978-3-0365-7320-5

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https://mdpi.com/books/pdfview/book/7265

Contributor(s)

Kuwajima, Kunihiro (editor)

Okamoto, Yuko (editor)

Knowles, Tuomas (editor)

Vendruscolo, Michele (editor)

Language

English

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Abstract

This Special Issue is dedicated to the memory of the late Professor Sir Christopher M. Dobson (1949–2019), who made outstanding contributions to the advancement of studies on protein folding and its related areas and played an irreplaceable role in the promotion of protein science. This reprint contains 24 recent research papers (17 original papers and 7 review papers) on protein folding, misfolding, and amyloid formation, which often lead to various human diseases.

URI

https://directory.doabooks.org/handle/20.500.12854/100802

Keywords

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