Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA.

@article{Hong1993StudiesOT,
  title={Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA.},
  author={Lin Hong and Gary P. Schroth and H. R. Matthews and Patrick Yau and E. Morton Bradbury},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 1},
  pages={
          305-14
        }
}
The effect of acetylation on the DNA binding properties of the rigidly conserved histone H4 amino-terminal tail has been studied in detail using the technique of thermal denaturation. The quantitative DNA-binding parameters for both the non- and fully acetylated H4 amino terminus have been determined from thermal denaturation data for complexes of the peptides bound to mixed sequence 146-base pair DNA. We find that under dilute buffer conditions (5 mM Tris-HCl) the binding constant for the non… CONTINUE READING

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