Date of Award

Spring 1985

Document Type

Thesis

Department

Life & Environmental Sciences

First Advisor

E. Morton Bradbury

Second Advisor

James Manion

Third Advisor

James Trudnowski

Abstract

The 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

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