Ontology highlight
ABSTRACT:
SUBMITTER: Sugiyama M
PROVIDER: S-EPMC4052288 | biostudies-literature | 2014 May
REPOSITORIES: biostudies-literature
Biophysical journal 20140501 10
Nucleosomes containing a human histone variant, H2A.B, in an aqueous solution were analyzed by small-angle neutron scattering utilizing a contrast variation technique. Comparisons with the canonical H2A nucleosome structure revealed that the DNA termini of the H2A.B nucleosome are detached from the histone core surface, and flexibly expanded toward the solvent. In contrast, the histone tails are compacted in H2A.B nucleosomes compared to those in canonical H2A nucleosomes, suggesting that they b ...[more]