Urea perturbation and the reversibility of nucleohistone conformation.
Urea effect on conformation and thermal stabilities in nucleohistone and NaCl-treated partially dehistonized nucleohistones has been studied by circular dichroism (CD) and thermal denaturation. Urea imposes a CD change at 278mm of DNA base pairs in native and NaCl-treated nucleohistones which can be decomposed into two parts: a decrease in Deltaepsilon(278) for histone-free base pairs and an increase for histone-bound base pairs. The reduction by urea of Deltaepsilon(220) of bound histones is approximately proportional to the increase of Deltaepsilon(278) of histone-bound base pairs. Urea also lowers the melting temperatures of base pairs both free and bound by histones. The presence of urea indeed destroys the secondary structure of bound histones, causing changes in the conformation and thermal stabilities of histone-bound base pairs in nucleohistone. Such a urea perturbation on nucleohistone conformation is reversible.
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D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004355:Drug Stability; D006657:Histones / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D013816:Thermodynamics; D014508:Urea
D006657:Histones; D014508:Urea