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DC Field | Value | Language |
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dc.contributor.author | Soni, G.V. | - |
dc.contributor.author | Brar, Loveleen | - |
dc.contributor.author | Hameed, F.M. | - |
dc.contributor.author | Raychaudhuri, A.K. | - |
dc.contributor.author | Shivashankar, G.V. | - |
dc.date.accessioned | 2008-10-31T11:11:10Z | - |
dc.date.available | 2008-10-31T11:11:10Z | - |
dc.date.issued | 2007-04 | - |
dc.identifier.citation | Applied Physics Letters, 2007, Vol.90, p163904 | en |
dc.identifier.issn | E-ISSN: 1077-3118 | - |
dc.identifier.issn | P-ISSN: 0003-6951 | - |
dc.identifier.uri | http://hdl.handle.net/2289/3660 | - |
dc.description | Open Access | en |
dc.description.abstract | Mechanical 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.extent | 379457 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | en | en |
dc.publisher | American Institute of Physics (AIP) | en |
dc.relation.uri | http://dx.doi.org/10.1063/1.2728031 | en |
dc.rights | 2007 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.title | Distinct levels in the nanoscale organization of DNA-histone complex revealed by its mechanical unfolding | en |
dc.type | Article | en |
Appears in Collections: | Research Papers (SCM) |
Files in This Item:
File | Description | Size | Format | |
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2007 ApplPhysLett_V90_p163904.pdf | Open Access | 370.56 kB | Adobe PDF | View/Open |
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