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Please use this identifier to cite or link to this item: https://doi.org/10.1103/PhysRevLett.95.208101
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dc.titleLow-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein fis
dc.contributor.authorSkoko, D.
dc.contributor.authorYan, J.
dc.contributor.authorJohnson, R.C.
dc.contributor.authorMarko, J.F.
dc.date.accessioned2014-10-16T09:31:20Z
dc.date.available2014-10-16T09:31:20Z
dc.date.issued2005-11-11
dc.identifier.citationSkoko, D., Yan, J., Johnson, R.C., Marko, J.F. (2005-11-11). Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein fis. Physical Review Letters 95 (20) : -. ScholarBank@NUS Repository. https://doi.org/10.1103/PhysRevLett.95.208101
dc.identifier.issn00319007
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/97106
dc.description.abstractWe report single-DNA-stretching experiments showing that the protein Fis, an abundant bacterial chromosome protein of E. coli, mediates a dramatic DNA condensation to zero length. This condensation occurs abruptly when DNA tension is reduced below a protein-concentration-dependent threshold f*
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1103/PhysRevLett.95.208101
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentPHYSICS
dc.description.doi10.1103/PhysRevLett.95.208101
dc.description.sourcetitlePhysical Review Letters
dc.description.volume95
dc.description.issue20
dc.description.page-
dc.description.codenPRLTA
dc.identifier.isiut000233243500068
Appears in Collections:Staff Publications

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