DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chong, LT | ko |
dc.contributor.author | Snow, CD | ko |
dc.contributor.author | Rhee, YM | ko |
dc.contributor.author | Pande, VS | ko |
dc.date.accessioned | 2017-08-16T08:55:56Z | - |
dc.date.available | 2017-08-16T08:55:56Z | - |
dc.date.created | 2017-08-07 | - |
dc.date.created | 2017-08-07 | - |
dc.date.issued | 2005-01 | - |
dc.identifier.citation | JOURNAL OF MOLECULAR BIOLOGY, v.345, no.4, pp.869 - 878 | - |
dc.identifier.issn | 0022-2836 | - |
dc.identifier.uri | http://hdl.handle.net/10203/225418 | - |
dc.description.abstract | Dimerization of the p53 oligomerization domain involves coupled folding and binding of monomers. To examine the dimerization, we have performed molecular dynamics (MD) simulations of dimer folding from the rate-limiting transition state ensemble (TSE). Among 799 putative transition state structures that were selected from a large ensemble of high-temperature unfolding trajectories, 129 were identified as members of the TSE via calculation of a 50% transmission coefficient from at least 20 room-temperature simulations. This study is the first to examine the refolding of a protein dimer using MD simulations in explicit water, revealing a folding nucleus for dimerization. Our atomistic simulations are consistent with experiment and offer insight that was previously unobtainable. (C) 2004 Elsevier Ltd. All rights reserved. | - |
dc.language | English | - |
dc.publisher | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | - |
dc.subject | TUMOR-SUPPRESSOR P53 | - |
dc.subject | TRANSITION-STATE | - |
dc.subject | TETRAMERIZATION DOMAIN | - |
dc.subject | UNSTRUCTURED PROTEINS | - |
dc.subject | MECHANISM | - |
dc.subject | BINDING | - |
dc.subject | RECOGNITION | - |
dc.subject | NUCLEATION | - |
dc.subject | ENSEMBLE | - |
dc.subject | WATER | - |
dc.title | Dimerization of the p53 oligomerization domain: Identification of a folding nucleus by molecular dynamics simulations | - |
dc.type | Article | - |
dc.identifier.wosid | 000225909100019 | - |
dc.identifier.scopusid | 2-s2.0-10044265557 | - |
dc.type.rims | ART | - |
dc.citation.volume | 345 | - |
dc.citation.issue | 4 | - |
dc.citation.beginningpage | 869 | - |
dc.citation.endingpage | 878 | - |
dc.citation.publicationname | JOURNAL OF MOLECULAR BIOLOGY | - |
dc.identifier.doi | 10.1016/j.jmb.2004.10.083 | - |
dc.contributor.localauthor | Rhee, YM | - |
dc.contributor.nonIdAuthor | Chong, LT | - |
dc.contributor.nonIdAuthor | Snow, CD | - |
dc.contributor.nonIdAuthor | Pande, VS | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | tumor suppressor p53 | - |
dc.subject.keywordAuthor | oligomerization | - |
dc.subject.keywordAuthor | protein folding | - |
dc.subject.keywordAuthor | protein interactions | - |
dc.subject.keywordAuthor | molecular dynamics simulation | - |
dc.subject.keywordPlus | TUMOR-SUPPRESSOR P53 | - |
dc.subject.keywordPlus | TRANSITION-STATE | - |
dc.subject.keywordPlus | TETRAMERIZATION DOMAIN | - |
dc.subject.keywordPlus | UNSTRUCTURED PROTEINS | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | NUCLEATION | - |
dc.subject.keywordPlus | ENSEMBLE | - |
dc.subject.keywordPlus | WATER | - |
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