title: Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. The conformation of phi1 histones from marine invertebrate sperm.
abstract: Proton magnetic resonance, circular dichroism and infrared spectroscopy are used to investigate the secondary and tertiary structure of three very lysine-rich histones from marine invertebrate sperm. At high ionic strength both Arbacia lixula and Holothuria tubulosa histone phi 1 are observed to contain 25-30% alpha-helix, no beta-structure and to form specific folded structures. Both phi 1 proton magnetic resonance spectra have perturbed methyl resonances at chemical shifts close to those observed for calf thymus H1, suggesting analogies in tertiary structure. Mytilus edulis histone phi 1 however, shows no spectroscopic evidence of secondary and tertiary structure on salt addition.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001974:Bromosuccinimide; D002843:Chromatin / Q000032:analysis* / Q000648:ultrastructure; D002942:Circular Dichroism; D004447:Echinodermata / Q000032:analysis*; D006657:Histones; D008239:Lysine / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D008974:Mollusca / Q000032:analysis*; D011487:Protein Conformation; D012617:Sea Urchins / Q000032:analysis*; D012623:Seawater; D013045:Species Specificity; D013094:Spermatozoa / Q000032:analysis*
chemical_list: D000596:Amino Acids; D002843:Chromatin; D006657:Histones; D008239:Lysine; D001974:Bromosuccinimide