Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA.
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.
D000818:Animals; D002417:Cattle; D002868:Chromosomal Proteins, Non-Histone; D002942:Circular Dichroism; D004247:DNA; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D011487:Protein Conformation
D002868:Chromosomal Proteins, Non-Histone; D004247:DNA