Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019)
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 cont...
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| Định dạng: | Online |
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| Ngôn ngữ: | Tiếng Anh |
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MDPI - Multidisciplinary Digital Publishing Institute
2023
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| Truy cập trực tuyến: | ONIX_20230623_9783036573212_34 |
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| _version_ | 1869530994935070720 |
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| collection | Directory of Open Access Books |
| description | 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. |
| format | Online |
| id | doab-20.500.12854ir-100802 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2023 |
| publishDateRange | 2023 |
| publishDateSort | 2023 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | ojs |
| spelling | doab-20.500.12854ir-1008022024-03-28T03:30:40Z Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019) Kuwajima, Kunihiro Okamoto, Yuko Knowles, Tuomas Vendruscolo, Michele 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 thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences 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. 2023-06-23T09:43:24Z 2023-06-23T09:43:24Z 2023 book ONIX_20230623_9783036573212_34 9783036573212 9783036573205 https://directory.doabooks.org/handle/20.500.12854/100802 eng image/jpeg Attribution 4.0 International https://mdpi.com/books/pdfview/book/7265 https://mdpi.com/books/pdfview/book/7265 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-0365-7320-5 10.3390/books978-3-0365-7320-5 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783036573212 9783036573205 418 Basel open access |
| spellingShingle | 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 thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019) |
| title | Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019) |
| title_full | Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019) |
| title_fullStr | Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019) |
| title_full_unstemmed | Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019) |
| title_short | Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019) |
| title_sort | frontiers in protein folding and related areas in memory of professor sir christopher m dobson 1949 2019 |
| topic | 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 thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| topic_facet | 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 thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| url | ONIX_20230623_9783036573212_34 |