TY - JOUR
T1 - 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
AU - PUIGDOMÉNECH, Pedro
AU - CABRÉ, Oriol
AU - PALAU, Jaime
AU - BRADBURY, E. Morton
AU - CRANE‐ROBINSON, Colyn
PY - 1975/1/1
Y1 - 1975/1/1
N2 - 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
AB - 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
U2 - 10.1111/j.1432-1033.1975.tb02447.x
DO - 10.1111/j.1432-1033.1975.tb02447.x
M3 - Article
VL - 59
SP - 237
EP - 243
IS - 1
ER -
