title: Physicochemical studies of non-histone protein HMG17 with DNA.
abstract: Non-histone protein high mobility group-17 (HMG17) isolated from calf thymus consists of 89 amino acids and the complete sequence is known (Walker, J.M., Hastings, J.R.B. and Johns, E.W. (1977) Eur. J. Biochem. 176, 461-468). We have studied its conformation and interaction with DNA by a variety of technics. The results show that the protein has a random structure. It binds non-cooperatively, non-specifically and reversibly to DNA. It is estimated that each molecule of protein binds to 57 nucleotides of calf thymus DNA. The equilibrium constant for binding is approx. 1 - 10(6) M-1. HMG17 induces conformational changes in DNA similar to some of the histones in particular H1.
mesh_terms: D000818:Animals; D002417:Cattle; D002868:Chromosomal Proteins, Non-Histone; D002942:Circular Dichroism; D004247:DNA; D007700:Kinetics; D008970:Molecular Weight; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D013696:Temperature; D013950:Thymus Gland
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D004247:DNA