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. 1978 Mar;84(1):173-7.
doi: 10.1111/j.1432-1033.1978.tb12154.x.

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

B D Abercrombie, G G Kneale, C Crane-Robinson, E M Bradbury, G H Goodwin, J M Walker, E W Johns
Free article

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

B D Abercrombie et al. Eur J Biochem. 1978 Mar.
Free article

Abstract

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 high protein/DNA ratio. The nuclear magnetic resonance data suggest that the principle DNA-binding segment of HMG 17 is that between about residues 15 and 40.

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