Physical studies of the nonhistone chromosomal proteins HMG-U and HMG-2.
Biochemistry, 1976/4/20;15(8):1645-9.
Baker C, Isenberg I, Goodwin GH, Johns EW
PMID: 5107
Impact factor: 3.321
Abstract
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.
MeSH terms
Animals; Binding Sites; Cattle; Chromosomes; Circular Dichroism; Dithiothreitol; Hydrogen-Ion Concentration; Nucleoproteins; Protein Binding; Protein Conformation; Sodium Chloride; Spectrophotometry, Ultraviolet; Thymus Gland
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