Properties of the N-Terminal 60-kDa-Fragment of Elongation Factor 2

K. V. Korotkov, A. N. Plotnikov, L. P. Motuz, K. S. Vasilenko, G. V. Semisotnov, Yu B. Alakhov

Research output: Contribution to journalArticlepeer-review


The N-terminal 60-kDa-fragment of elongation factor 2 from rat liver (EF-2) was obtained by the limited proteolysis of native EF-2 with elastase. This fragment consists of 506 N-terminal amino acid residues of EF-2. The conformational properties of both this fragment and EF-2 in solution were studied by circular dichroism and fluorescent spectroscopy. The contents of secondary structure components in the fragment and in the factor that were deduced from CD measurements agreed well with values predicted from their primary structures. Both proteins were resistant to denaturation with ≤3 M urea and exhibited cooperative denaturation transitions. Temperature melting also proceeded cooperatively for the fragment and EF-2. Structural properties of the N-terminal 60-kDa-fragment are discussed in comparison with the biochemical characteristics and 3D structure of prokaryotic elongation factor EF-G.

Original languageEnglish
Pages (from-to)174
Number of pages1
JournalBioorganicheskaya Khimiya
Issue number3
StatePublished - Mar 1998


  • Elongation factor 2
  • Limited proteolysis
  • Protein fragments

ASJC Scopus subject areas

  • General Medicine


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