Please use this identifier to cite or link to this item: http://hdl.handle.net/2289/3660
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dc.contributor.authorSoni, G.V.-
dc.contributor.authorBrar, Loveleen-
dc.contributor.authorHameed, F.M.-
dc.contributor.authorRaychaudhuri, A.K.-
dc.contributor.authorShivashankar, G.V.-
dc.date.accessioned2008-10-31T11:11:10Z-
dc.date.available2008-10-31T11:11:10Z-
dc.date.issued2007-04-
dc.identifier.citationApplied Physics Letters, 2007, Vol.90, p163904en
dc.identifier.issnE-ISSN: 1077-3118-
dc.identifier.issnP-ISSN: 0003-6951-
dc.identifier.urihttp://hdl.handle.net/2289/3660-
dc.descriptionOpen Accessen
dc.description.abstractMechanical unfolding of nanoscale DNA-histone complex, using an atomic force microscope, shows a stepwise disassembly of histones from the nucleosome. A quantitative analysis of the rupture jump statistics and the length released per jump reveals insights into the possible histone contacts within the octamer complex. The measured ruptures correlate with the breakage of multiple contacts that stabilize the histone octamer. These results provide a mechanistic basis by which stepwise disassembly of histone proteins may result from an external force exerted by the adenosinetriphosphate (ATP) dependent chromatin remodeling machines to access regulatory sites on DNA.en
dc.format.extent379457 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.publisherAmerican Institute of Physics (AIP)en
dc.relation.urihttp://dx.doi.org/10.1063/1.2728031en
dc.rights2007 American Institute of Physics. This article may be downloaded for personal use only. Any other use requires prior permission of the author and the American Institute of Physics.en
dc.titleDistinct levels in the nanoscale organization of DNA-histone complex revealed by its mechanical unfoldingen
dc.typeArticleen
Appears in Collections:Research Papers (SCM)

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