Corpus ID: 8920894

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={L. Hong and G. Schroth and H. R. Matthews and P. Yau and E. M. Bradbury},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 1},
  pages={
          305-14
        }
}
  • L. Hong, G. Schroth, +2 authors E. M. Bradbury
  • Published 1993
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 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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