Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy.
The secondary structure of histones H1, H2A, and H4 (F1, F2a2, and F2a1) has been quantitatively studied in heavy water (2H2O) solutions in a wide range of histone concentration, p2H, and concentration of sodium chloride using an improved infrared spectroscopy method. Under all conditions there are about 5--10% of alpha helix. Conditions favourable for aggregation induce formation of antiparallel pleated sheet structure to an extent of about 15% in H1 and H2A and about 30% in H4. When the p2H and concentration of NaCl are in the physiological range, there is the same content of this structure in H2A and H4 and none in H1.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D006657:Histones; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D011487:Protein Conformation; D012965:Sodium Chloride; D013055:Spectrophotometry, Infrared; D013950:Thymus Gland
D006657:Histones; D012965:Sodium Chloride