A NMR study of mobility in the histone octamer

Gary P. Schroth, Peter Yau, Brian S. Imai, Joe M. Gatewood, E. Morton Bradbury

Research output: Contribution to journalArticlepeer-review


The histone octamer from chicken erythrocytes was studied in 2 M NaCI using 500 mHz 1H NMR spectroscopy. We compared the spectrum of control octamers with that of octamers isolated from trypsinized nucleosome core particles. We observe that the sharp resonances found in the spectrum of the native octamer disappear completely after trypsinization. Therefore, within the time frame of the NMR experiment, all of the mobile amino acid residues in the histone octamer are found in the well defined trypsin sensitive domains. These results indicate that there is a very clear structural demarcation between the random coil N- and C-terminal tails and the globular domains of the histones.

Original languageEnglish (US)
Pages (from-to)117-120
Number of pages4
JournalFEBS Letters
Issue number1
StatePublished - Jul 30 1990
Externally publishedYes


  • Chromatin
  • Histone octamer
  • Nuclear magnetic resonance
  • Trypsin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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