A nuclear-magnetic-resonance study of the globular structure of the H5 histone.
The structure of the globular region of the chicken erythrocyte H5 histone has been studied by 270-MHz proton magnetic resonance. The aromatic resonances have been partially assigned by a combination of selective deuteration and iodination with the nuclear magnetic resonance spectroscopy. Detailed titration studies have revealed interactions between residues in the structure. A technique involving the measurement of small nuclear Overhauser effects has enabled  the assignment of the aromatic residues causing the perturbation of the ring-current-shifted methyl resonances occurring in the upfield region of the spectrum. Spin-decoupling experiments on these peaks has enabled a partial assignment of shifted methyl resonances. The results support the notion that the histone H5 globular structure is different from that of the homologous histone H1 molecule.
D000818:Animals; D002645:Chickens; D004912:Erythrocytes / Q000032:analysis; D006639:Histidine; D006657:Histones / Q000097:blood; D009682:Magnetic Resonance Spectroscopy; D009994:Osmolar Concentration; D010446:Peptide Fragments; D011487:Protein Conformation
D006657:Histones; D010446:Peptide Fragments; D006639:Histidine