Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules
DC Field | Value | Language |
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dc.contributor.author | Choi, Hyunsung | - |
dc.contributor.author | Chang, Hyun Joon | - |
dc.contributor.author | Lee, Myeongsang | - |
dc.contributor.author | Na, Sungsoo | - |
dc.date.accessioned | 2021-09-03T07:14:33Z | - |
dc.date.available | 2021-09-03T07:14:33Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017-04-05 | - |
dc.identifier.issn | 1439-4235 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/83777 | - |
dc.description.abstract | In biological systems, structural confinements of amyloid fibrils can be mediated by the role of water molecules. However, the underlying effect of the dynamic behavior of water molecules on structural stabilities of amyloid fibrils is still unclear. By performing molecular dynamics simulations, we investigate the dynamic features and the effect of interior water molecules on conformations and mechanical characteristics of various amyloid fibrils. We find that a specific mechanism induced by the dynamic properties of interior water molecules can affect diffusion of water molecules inside amyloid fibrils, inducing their different structural stabilities. The conformation of amyloid fibrils induced by interior water molecules show the fibrils' different mechanical features. We elucidate the role of confined and movable interior water molecules in structural stabilities of various amyloid fibrils. Our results offer insights not only in further understanding of mechanical features of amyloids as mediated by water molecules, but also in the fine-tuning of the functional abilities of amyloid fibrils for applications. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | WILEY-V C H VERLAG GMBH | - |
dc.subject | ATOMIC-FORCE MICROSCOPY | - |
dc.subject | A-BETA-PEPTIDE | - |
dc.subject | ALZHEIMERS-DISEASE | - |
dc.subject | CONFORMATIONAL-CHANGES | - |
dc.subject | MECHANICAL-PROPERTIES | - |
dc.subject | DYNAMICS SIMULATION | - |
dc.subject | PROTEIN AGGREGATION | - |
dc.subject | PHYSIOLOGICAL PH | - |
dc.subject | LYSINE RESIDUES | - |
dc.subject | TAU-PROTEIN | - |
dc.title | Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Na, Sungsoo | - |
dc.identifier.doi | 10.1002/cphc.201601327 | - |
dc.identifier.scopusid | 2-s2.0-85013632849 | - |
dc.identifier.wosid | 000402711100013 | - |
dc.identifier.bibliographicCitation | CHEMPHYSCHEM, v.18, no.7, pp.817 - 827 | - |
dc.relation.isPartOf | CHEMPHYSCHEM | - |
dc.citation.title | CHEMPHYSCHEM | - |
dc.citation.volume | 18 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 817 | - |
dc.citation.endPage | 827 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalResearchArea | Physics | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Physical | - |
dc.relation.journalWebOfScienceCategory | Physics, Atomic, Molecular & Chemical | - |
dc.subject.keywordPlus | ATOMIC-FORCE MICROSCOPY | - |
dc.subject.keywordPlus | A-BETA-PEPTIDE | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | CONFORMATIONAL-CHANGES | - |
dc.subject.keywordPlus | MECHANICAL-PROPERTIES | - |
dc.subject.keywordPlus | DYNAMICS SIMULATION | - |
dc.subject.keywordPlus | PROTEIN AGGREGATION | - |
dc.subject.keywordPlus | PHYSIOLOGICAL PH | - |
dc.subject.keywordPlus | LYSINE RESIDUES | - |
dc.subject.keywordPlus | TAU-PROTEIN | - |
dc.subject.keywordAuthor | confined water | - |
dc.subject.keywordAuthor | heterogeneous amyloid fibril | - |
dc.subject.keywordAuthor | mechanical properties | - |
dc.subject.keywordAuthor | molecular dynamics | - |
dc.subject.keywordAuthor | steered molecular dynamics | - |
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