Baker C, Isenberg I, Goodwin G H, Johns E W
Biochemistry. 1976 Apr 20;15(8):1645-9. doi: 10.1021/bi00653a009.
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.
非组蛋白染色体蛋白HMG - 1和HMG - 2在很宽的pH范围内具有折叠构象，α - 螺旋含量高。在高pH值和低pH值时，分子会展开。这两种分子都含有半胱氨酸和色氨酸。色氨酸似乎以折叠形式被掩埋。HMG - 1在pH 5.7时出现聚集，HMG - 2在pH 9.0时也会如此。折叠形式对高浓度盐不敏感，这表明电荷 - 电荷相互作用在稳定三级结构中不起作用。
