Aug 1, 1976

Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy

European Journal of Biochemistry
B V Shestopalov, Y N Chirgadze

Abstract

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.

Mentioned in this Paper

Plasma Protein Binding Capacity
Infrared Spectrophotometry
Protein Conformation
Sodium Chloride, (24)NaCl
Bos indicus
Histone H7
Hydrogen-Ion Concentration
Thymus Gland

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