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DC Field | Value | Language |
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dc.citation.endPage | 6831 | - |
dc.citation.number | 23 | - |
dc.citation.startPage | 6819 | - |
dc.citation.title | JOURNAL OF PHYSICAL CHEMISTRY B | - |
dc.citation.volume | 116 | - |
dc.contributor.author | Chen, Ke | - |
dc.contributor.author | Eargle, John | - |
dc.contributor.author | Lai, Jonathan | - |
dc.contributor.author | Kim, Hajin | - |
dc.contributor.author | Abeysirigunawardena, Sanjaya | - |
dc.contributor.author | Mayerle, Megan | - |
dc.contributor.author | Woodson, Sarah | - |
dc.contributor.author | Ha, Taekjip | - |
dc.contributor.author | Luthey-Schulten, Zaida | - |
dc.date.accessioned | 2023-12-22T05:07:58Z | - |
dc.date.available | 2023-12-22T05:07:58Z | - |
dc.date.created | 2014-10-10 | - |
dc.date.issued | 2012-06 | - |
dc.description.abstract | Assembly of the bacterial ribosomal small subunit (SSU) begins with the folding of the five-way junction upon interaction with the primary binding protein S4. This complex contains the largest contiguous molecular signature, which is a conserved feature in all bacterial 16S rRNAs. In a previous study, we used all-atom molecular dynamics simulations to demonstrate that the co-evolving signature in the N-terminus of S4 is intrinsically disordered and capable of accelerating the binding process through a fly casting mechanism. In this paper, comparisons between the all-atom MD simulations and FRET experiments identify multiple metastable conformations of the naked five-way junction without the presence of S4. Furthermore, we capture the simultaneous folding and binding of the five-way junction and r-protein S4 by use of a structure-based Gō potential implemented within the framework of the all-atom molecular dynamics CHARMM force field. Different folding pathways are observed for the refolding of the five-way junction upon partial binding of S4. Our simulations illustrate the complex nature of RNA folding in the presence of a protein binding partner and provide insight into the role of population shift and the induced fit mechanisms in the protein:RNA folding and binding process. | - |
dc.identifier.bibliographicCitation | JOURNAL OF PHYSICAL CHEMISTRY B, v.116, no.23, pp.6819 - 6831 | - |
dc.identifier.doi | 10.1021/jp212614b | - |
dc.identifier.issn | 1520-6106 | - |
dc.identifier.scopusid | 2-s2.0-84862271578 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/7106 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84862271578 | - |
dc.identifier.wosid | 000305356100027 | - |
dc.language | 영어 | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Assembly of the Five-Way Junction in the Ribosomal Small Subunit Using Hybrid MD-Go Simulations | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | SELECTIVE 2&apos | - |
dc.subject.keywordPlus | -HYDROXYL ACYLATION | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI RIBOSOMES | - |
dc.subject.keywordPlus | PROTEIN S4 | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS | - |
dc.subject.keywordPlus | FOLDING LANDSCAPE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | SINGLE MOLECULES | - |
dc.subject.keywordPlus | NATIVE TOPOLOGY | - |
dc.subject.keywordPlus | DOMAINS ARCHAEA | - |
dc.subject.keywordPlus | TRANSFER-RNA | - |
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