ECB-ART-30938
Eur J Biochem
1975 Nov 01;591:237-43. doi: 10.1111/j.1432-1033.1975.tb02447.x.
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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.
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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.
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Genes referenced: LOC579470