Conformational Entropy of Intrinsically Disordered Protein
DC Field | Value | Language |
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dc.contributor.author | Chong, Song-Ho | - |
dc.contributor.author | Ham, Sihyun | - |
dc.date.available | 2021-02-22T12:16:07Z | - |
dc.date.issued | 2013-05 | - |
dc.identifier.issn | 1520-6106 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/11280 | - |
dc.description.abstract | Intrinsically disordered proteins (IDPs), though lacking stable tertiary structures, are known to possess a certain amount of residual structure. Conformational disorder plays a crucial role through the conformational entropy in regulating protein-protein and protein ligand interactions involved in signaling and regulation, and also modulates protein aggregation and amyloidogenesis associated with a number of human diseases. However, a direct and quantitative connection between the residual structure and the conformational entropy remains to be established. Here we show using a novel computational approach that the conformational entropy of amyloid-beta protein, an IDP whose aggregation is associated with Alzheimer's disease, is significantly correlated with the contents of the residual helical structure, beta-sheet structure, and salt-bridge network. Identification of the thermodynamically significant residual structure is of fundamental importance for a comprehensive understanding of the relationship between the functional conformational disorder and the protein activity regulation, and will also serve the thermodynamic basis of the amyloid polymorphism. | - |
dc.format.extent | 7 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Conformational Entropy of Intrinsically Disordered Protein | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1021/jp401049h | - |
dc.identifier.scopusid | 2-s2.0-84877694532 | - |
dc.identifier.wosid | 000318891700011 | - |
dc.identifier.bibliographicCitation | JOURNAL OF PHYSICAL CHEMISTRY B, v.117, no.18, pp 5503 - 5509 | - |
dc.citation.title | JOURNAL OF PHYSICAL CHEMISTRY B | - |
dc.citation.volume | 117 | - |
dc.citation.number | 18 | - |
dc.citation.startPage | 5503 | - |
dc.citation.endPage | 5509 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Physical | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | FREE-ENERGY | - |
dc.subject.keywordPlus | THERMODYNAMICS | - |
dc.subject.keywordPlus | POLYMORPHISM | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | SIMULATIONS | - |
dc.subject.keywordPlus | FLEXIBILITY | - |
dc.subject.keywordPlus | MODEL | - |
dc.identifier.url | https://pubs.acs.org/doi/10.1021/jp401049h | - |
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