| Literature DB >> 565710 |
B D Abercrombie, G G Kneale, C Crane-Robinson, E M Bradbury, G H Goodwin, J M Walker, E W Johns.
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.Entities:
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Year: 1978 PMID： 565710 DOI： 10.1111/j.1432-1033.1978.tb12154.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956