Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA.

@article{Abercrombie1978StudiesOT,
  title={Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA.},
  author={B D Abercrombie and G. Geoff Kneale and Colyn Crane-Robinson and E. Morton Bradbury and G. H. Goodwin and J Michael Walker and E. W. Johns},
  journal={European journal of biochemistry},
  year={1978},
  volume={84 1},
  pages={173-7}
}
The conformation of the non-histone chromatin protein, HMG 17, has been studied using circular dichroism, infrared and nuclear magnetic resonance spectroscopies, and by small-angle scattering. The results show that in free solution this protein has little or no secondary or tertiary structure in contrast to the other high-mobility-group proteins, HMG 1 and 2, which exhibit highly ordered structures. Protein HMG 17 binds to calf thymus DNA in an ionic-dependent manner, precipitating the DNA at… CONTINUE READING