Transient Unfolding of Trypsin‐Digested Chromatin Core Particles

Sergei A. GRIGORYEV, Igor A. KRASHENINNIKOV

Research output: Contribution to journalArticle

14 Citations (Scopus)

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

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Nucleosomes
Chromatin
Histones
Nucleoproteins
Dichroism
Circular Dichroism
Sedimentation
Trypsin
Digestion
Amino Acid Sequence
Assays
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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Transient Unfolding of Trypsin‐Digested Chromatin Core Particles. / GRIGORYEV, Sergei A.; KRASHENINNIKOV, Igor A.

In: European Journal of Biochemistry, Vol. 129, No. 1, 12.1982, p. 119-125.

Research output: Contribution to journalArticle

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