The histone octamer, a conformationally flexible structure.
The conformation of the histone octamer complex in solution has been shown, by circular dichroism studies, to be highly dependent on the nature of the salt milieu and its concentration. In 2 M NaCl, the complex has 43.5% alpha-helix, 16% beta-sheet, and 40.5% random structure. In 2.3 M (NH4)2SO4, the octamer has 49.0% alpha-helix and 51% random structure. These results partially explain the discrepant results obtained by the X-ray analysis of crystals obtained under varying conditions.
Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254.
K
K
Park
G D
GD
Fasman
D000645:Ammonium Sulfate / Q000494:pharmacology; D000818:Animals; D002645:Chickens; D002942:Circular Dichroism; D004912:Erythrocytes / Q000378:metabolism; D006657:Histones / Q000097:blood / Q000302:isolation & purification; D046911:Macromolecular Substances; D009994:Osmolar Concentration; D011487:Protein Conformation; D012965:Sodium Chloride / Q000494:pharmacology
D006657:Histones; D046911:Macromolecular Substances; D012965:Sodium Chloride; D000645:Ammonium Sulfate