Physical studies of the nonhistone chromosomal proteins HMG-U and HMG-2.
The nonhistone chromosomal proteins, HMG-1 and HMG-2, have a folded conformation, with a high alpha-helical content, over a wide pH range. At high and low pH values, the molecules unfold. Both molecules contain cysteine and tryptophan. The tryptophans appear to be buried in the folded form. HMG-1 shows aggregation at pH 5.7, as does HMG-2 at pH 9.0. The folded form is insensitive to high concentrations of salt, suggesting that charge-charge interaction plays no role in stabilizing the tertiary structure.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002875:Chromosomes / Q000032:analysis*; D002942:Circular Dichroism; D004229:Dithiothreitol; D006863:Hydrogen-Ion Concentration; D009698:Nucleoproteins; D011485:Protein Binding; D011487:Protein Conformation; D012965:Sodium Chloride; D013056:Spectrophotometry, Ultraviolet; D013950:Thymus Gland / Q000032:analysis
D009698:Nucleoproteins; D012965:Sodium Chloride; D004229:Dithiothreitol