PMID: 1204610Nov 1, 1975Paper

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

European Journal of Biochemistry
P PuigdoménechC Crane-Robinson

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.

References

Aug 30, 1972·Nature: New Biology·E M BradburyE W Johns
Mar 1, 1969·Archives of Biochemistry and Biophysics·S Panyim, R Chalkley
Jan 1, 1969·European Journal of Biochemistry·J PalauJ A Subirana
Jan 15, 1964·Experientia·L S Hnilica
Dec 1, 1964·Canadian Journal of Biochemistry·J M NEELINK MURRAY
Aug 30, 1973·Biochimica Et Biophysica Acta·J A SubiranaM Unzeta

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Citations

Jan 1, 1983·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·P Martínez, J Palau
Aug 1, 1983·European Journal of Biochemistry·E Brown, G H Goodwin
Oct 12, 1981·FEBS Letters·S H BrandI O Walker

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