Studies on the Role and Mode of Operation of the Very‐Lysine‐Rich Histones in Eukaryote Chromatin: The Conformation of ϕ 1 Histones from Marine Invertebrate Sperm

Pedro PUIGDOMÉNECH, Oriol CABRÉ, Jaime PALAU, E. Morton BRADBURY, Colyn CRANE‐ROBINSON

Research output: Contribution to journalArticleResearchpeer-review

13 Citations (Scopus)

Abstract

Proton magnetic resonance, circular dichroism and infrared spectroscopy are used to investigate the secondary and tertiary structures of three very lysine‐rich histones from marine invertebrate sperm. At high ionic strength both Arbacia lixula and Holothuria tubulosa histone ϕ 1 are observed to contain 25–30%α‐helix, no β‐structure and to form specific folded structures. Both ϕ 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 ϕ 1 however, shows no spectroscopic evidence of secondary and tertiary structure on salt addition. Copyright © 1975, Wiley Blackwell. All rights reserved
Original languageEnglish
Pages (from-to)237-243
JournalEuropean Journal of Biochemistry
Volume59
Issue number1
DOIs
Publication statusPublished - 1 Jan 1975

Fingerprint Dive into the research topics of 'Studies on the Role and Mode of Operation of the Very‐Lysine‐Rich Histones in Eukaryote Chromatin: The Conformation of ϕ 1 Histones from Marine Invertebrate Sperm'. Together they form a unique fingerprint.

Cite this