Abstract
Binding constants have been measured for the interaction of the protein HMG1 with native DNA, denatured DNA and a number of polynucleotides at near-physiological ionic strengths, using gel filtration and thermal denaturation. The interaction of HMG1 with DNA is shown to be noncooperative and reversible. Nucleic acids form the following series in order of increasing binding constants: poly(U) ∞ poly(A) < poly(dA) < dsDNA ∞ poly(dA) · poly(dT) ∞ poly(dG) · poly(dC) « poly[d(A-T)] ∞ ssDNA.
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