doi: 10.1111/j.1432-1033.1976.tb10640.x.
Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy
- PMID: 9273
- DOI: 10.1111/j.1432-1033.1976.tb10640.x
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Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy
Eur J Biochem.
.
Free article
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.
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