Transient Unfolding of Trypsin‐Digested Chromatin Core Particles

Sergei A. GRIGORYEV, Igor A. KRASHENINNIKOV

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Limited digestion of nucleosome core particles with trypsin caused cleavage and removal of N‐terminal histone sequences of 10–30 amino acids. The proteolyzed core particles exhibited salt‐dependent structural transitions revealed by sedimentation, circular dichroism and nuclease‐cutting assays, while the intact nucleosome cores were not affected under the experimental conditions. The results obtained indicate that the observed transitions correspond to the transient unfolding of terminal segments of core particle nucleoprotein caused by the increase of its net negative charge. The excision of the N‐terminal histone domains therefore leads to partial destabilization but not to irreversible disruption of the compact nucleosome structure.

Original languageEnglish (US)
Pages (from-to)119-125
Number of pages7
JournalEuropean Journal of Biochemistry
Volume129
Issue number1
DOIs
StatePublished - Dec 1982

All Science Journal Classification (ASJC) codes

  • Biochemistry

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