Structural studies of chicken erythrocyte histone H5.
Spectroscopic studies (nuclear magnetic resonance, circular dichroism and infrared) have been carried out on chicken erythrocyte histone H5 and on  three peptides cleaved therefrom: 1-31, 32-197 and 58-197. It is shown that at ionic strengths above o.1M part of the H5 molecule takes up a globular conformation containing 14% alpha helix but no beta sheet structure. Several details of the circular dichroism and nuclear magnetic resonace spectra indicate that the globular region is located in the N-terminal half of the molecule and this proposal is supported by the observation that the peptide 32-197 is largely incapable of folding and the peptide 59-197 is completely incapable of folding. Structural similarities and differences between histone H5 and histone H1 are discussed.
D000818:Animals; D002942:Circular Dichroism; D004912:Erythrocytes / Q000032:analysis*; D006657:Histones / Q000097:blood; D009682:Magnetic Resonance Spectroscopy; D009994:Osmolar Concentration; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D011489:Protein Denaturation; D013055:Spectrophotometry, Infrared; D013696:Temperature
D006657:Histones; D010446:Peptide Fragments