Studies on the Conformational Properties of the High‐Mobility‐Group Chromosomal Protein HMG 17 and Its Interaction with DNA
Barry D. ABERCROMBIE, Geoffrey G. Kneale, Colyn Crane‐Robinson, E. Morton Bradbury, Graham H. Goodwin, John Malcolm Walker, Ernest W. Johns · European Journal of Biochemistry · 1978
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.