DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, WK | - |
dc.contributor.author | Jergic, S | - |
dc.contributor.author | Kim, D | - |
dc.contributor.author | Dixon, NE | - |
dc.contributor.author | Lee, JB | - |
dc.date.accessioned | 2016-03-31T07:30:10Z | - |
dc.date.available | 2016-03-31T07:30:10Z | - |
dc.date.created | 2015-02-17 | - |
dc.date.issued | 2014-06 | - |
dc.identifier.issn | 1433-7851 | - |
dc.identifier.other | 2014-OAK-0000032043 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/13702 | - |
dc.description.abstract | Sliding DNA clamps are loaded at a ss/dsDNA junction by a clamp loader that depends on ATP binding for clamp opening. Sequential ATP hydrolysis results in closure of the clamp so that it completely encircles and diffuses on dsDNA. We followed events during loading of an E. coli beta clamp in real time by using single-molecule FRET (smFRET). Three successive FRET states were retained for 0.3 s, 0.7 s, and 9 min: Hydrolysis of the first ATP molecule by the g clamp loader resulted in closure of the clamp in 0.3 s, and after 0.7 s in the closed conformation, the clamp was released to diffuse on the dsDNA for at least 9 min. An additional single-molecule polarization study revealed that the interfacial domain of the clamp rotated in plane by approximately 88 during clamp closure. The single-molecule polarization and FRET studies thus revealed the real-time dynamics of the ATP-hydrolysis-dependent 3D conformational change of the b clamp during loading at a ss/dsDNA junction. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | John Wiley & Sons Ltd. | - |
dc.relation.isPartOf | Angewandte Chemie - International Edition | - |
dc.title | Loading Dynamics of a sliding DNA clamp | - |
dc.type | Article | - |
dc.contributor.college | 물리학과 | - |
dc.identifier.doi | 10.1002/ANIE.201403063 | - |
dc.author.google | Cho, WK | - |
dc.author.google | Jergic, S | - |
dc.author.google | Kim, D | - |
dc.author.google | Dixon, NE | - |
dc.author.google | Lee, JB | - |
dc.relation.volume | 53 | - |
dc.relation.issue | 26 | - |
dc.relation.startpage | 6768 | - |
dc.relation.lastpage | 6771 | - |
dc.contributor.id | 10171158 | - |
dc.relation.journal | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Angewandte Chemie - International Edition, v.53, no.26, pp.6768 - 6771 | - |
dc.identifier.wosid | 000338021600035 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 6771 | - |
dc.citation.number | 26 | - |
dc.citation.startPage | 6768 | - |
dc.citation.title | Angewandte Chemie - International Edition | - |
dc.citation.volume | 53 | - |
dc.contributor.affiliatedAuthor | Lee, JB | - |
dc.identifier.scopusid | 2-s2.0-84903212525 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 5 | - |
dc.description.scptc | 6 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.description.isOpenAccess | Y | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | POLYMERASE-III HOLOENZYME | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | GAMMA-COMPLEX | - |
dc.subject.keywordPlus | ATP HYDROLYSIS | - |
dc.subject.keywordPlus | BETA-SUBUNIT | - |
dc.subject.keywordPlus | LOADER COMPLEX | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | REPLICATION | - |
dc.subject.keywordPlus | MACHINE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordAuthor | DNA clamps | - |
dc.subject.keywordAuthor | DNA replication | - |
dc.subject.keywordAuthor | single-molecule FRET | - |
dc.subject.keywordAuthor | single-molecule polarization | - |
dc.subject.keywordAuthor | ternary complexes | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
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