Morphology and mechanical properties of multi-stranded amyloid fibrils probed by atomistic and coarse-grained simulations
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Yoon, Gwonchan | - |
dc.contributor.author | Lee, Myeongsang | - |
dc.contributor.author | Kim, Kyungwoo | - |
dc.contributor.author | Kim, Jae In | - |
dc.contributor.author | Chang, Hyun Joon | - |
dc.contributor.author | Baek, Inchul | - |
dc.contributor.author | Eom, Kilho | - |
dc.contributor.author | Na, Sungsoo | - |
dc.date.accessioned | 2021-09-04T10:15:25Z | - |
dc.date.available | 2021-09-04T10:15:25Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2015-12 | - |
dc.identifier.issn | 1478-3967 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/91814 | - |
dc.description.abstract | Amyloid fibrils are responsible for pathogenesis of various diseases and exhibit the structural feature of an ordered, hierarchical structure such as multi-stranded helical structure. As the multi-strandedness of amyloid fibrils has recently been found to be highly correlated with their toxicity and infectivity, it is necessary to study how the hierarchical (i.e. multi-stranded) structure of amyloid fibril is formed. Moreover, although it has recently been reported that the nanomechanics of amyloid proteins plays a key role on the amyloid-induced pathogenesis, a critical role that the multi-stranded helical structure of the fibrils plays in their nanomechanical properties has not fully characterized. In this work, we characterize the morphology and mechanical properties of multi-stranded amyloid fibrils by using equilibrium molecular dynamics simulation and elastic network model. It is shown that the helical pitch of multi-stranded amyloid fibril is linearly proportional to the number of filaments comprising the amyloid fibril, and that multi-strandedness gives rise to improving the bending rigidity of the fibril. Moreover, we have also studied the morphology and mechanical properties of a single protofilament (filament) in order to understand the effect of cross-beta structure and mutation on the structures and mechanical properties of amyloid fibrils. Our study sheds light on the underlying design principles showing how the multi-stranded amyloid fibril is formed and how the structure of amyloid fibrils governs their nanomechanical properties. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | IOP PUBLISHING LTD | - |
dc.subject | MOLECULAR-DYNAMICS SIMULATION | - |
dc.subject | NORMAL-MODE ANALYSIS | - |
dc.subject | SOLID-STATE NMR | - |
dc.subject | FORCE MICROSCOPY | - |
dc.subject | PERSISTENCE LENGTH | - |
dc.subject | PROTEIN STRUCTURES | - |
dc.subject | 3D STRUCTURE | - |
dc.subject | IN-VITRO | - |
dc.subject | BETA(2)-MICROGLOBULIN | - |
dc.subject | NANOMECHANICS | - |
dc.title | Morphology and mechanical properties of multi-stranded amyloid fibrils probed by atomistic and coarse-grained simulations | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Na, Sungsoo | - |
dc.identifier.doi | 10.1088/1478-3975/12/6/066021 | - |
dc.identifier.scopusid | 2-s2.0-84953792284 | - |
dc.identifier.wosid | 000368186300027 | - |
dc.identifier.bibliographicCitation | PHYSICAL BIOLOGY, v.12, no.6 | - |
dc.relation.isPartOf | PHYSICAL BIOLOGY | - |
dc.citation.title | PHYSICAL BIOLOGY | - |
dc.citation.volume | 12 | - |
dc.citation.number | 6 | - |
dc.type.rims | ART | - |
dc.type.docType | Article; Proceedings Paper | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS SIMULATION | - |
dc.subject.keywordPlus | NORMAL-MODE ANALYSIS | - |
dc.subject.keywordPlus | SOLID-STATE NMR | - |
dc.subject.keywordPlus | FORCE MICROSCOPY | - |
dc.subject.keywordPlus | PERSISTENCE LENGTH | - |
dc.subject.keywordPlus | PROTEIN STRUCTURES | - |
dc.subject.keywordPlus | 3D STRUCTURE | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | BETA(2)-MICROGLOBULIN | - |
dc.subject.keywordPlus | NANOMECHANICS | - |
dc.subject.keywordAuthor | amyloid proteins | - |
dc.subject.keywordAuthor | multi-strandness | - |
dc.subject.keywordAuthor | normal mode analysis | - |
dc.subject.keywordAuthor | molecular dynamics | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.