Abstract
Conformation changes of poly (dA-dT) under various conditions of temperature, solvent, and in the presence of DNA polymerase from Micrococcus luteus, were investigated by means of circular dichroism. The interaction of poly (dA-dT) with these proteins is reflected in spectral changes, which indicates the stabilization of the secondary structure towards an ordered form, and which characterizes poly (dA-dT) at low temperature and high ionic strength. This form can be considered to be similar to the B form. Under the influence of an increasing concentration of ethylene glycol, poly (dA-dT), at low temperature, adopts different conformations when compared to its complex with proteins, and which is interpreted to be similar to the C form. Preliminary study of the interaction DNA-DNA polymerase shows the appearance of conformational changes when the complex is formed, and suggest the stabilization of AT rich regions.
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