The Effect Of The Linker DNA regions Of Mononucleosomes With Respect To Stability In Thermal Denaturation Analysis

carrollscholars.legacy.contextkey12467446
carrollscholars.legacy.itemurlhttps://scholars.carroll.edu/lifesci_theses/389
carrollscholars.object.degreeBachelor's
carrollscholars.object.departmentLife & Environmental Sciences
carrollscholars.object.disciplinesBiochemistry; Molecular Biology; Molecular Genetics; Structural Biology
carrollscholars.object.seasonSpring
dc.contributor.advisorE. Morton Bradbury
dc.contributor.advisorJames Manion
dc.contributor.advisorJames Trudnowski
dc.contributor.authorSalmassy, David
dc.date.accessioned2020-04-30T10:02:42Z
dc.date.available2020-04-30T10:02:42Z
dc.date.embargo12/31/1899 0:00
dc.date.issued1985-04-01
dc.description.abstractThe stability afforded to the mononucleosomal core complex on samples of chicken erythrocyte chromatin was studied. Samples of chromatin digested to mononucleosomal (145 + base pairs) and core particle lengths (145 base pairs) were used in a nonreconstituted and a reconstituted form using High Mobility Group protein 17 in a series of thermal denaturation melting studies. The results give evidence that the linker DMA regions extending into and out of the entry and exit sites of the mononucleosome may indeed enhance the stability of the complex against the melting. This can not be stated as an isolated fact because of the presence of histone protein Hi in the large sample fractions which may independently have its own effect on the stability of the complex
dc.identifier.urihttps://scholars.carroll.edu/handle/20.500.12647/3131
dc.titleThe Effect Of The Linker DNA regions Of Mononucleosomes With Respect To Stability In Thermal Denaturation Analysis
dc.typethesis
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