title: Structural studies of chicken erythrocyte histone H5.
abstract: 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.
mesh_terms: 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
chemical_list: D006657:Histones; D010446:Peptide Fragments