The Chloroplast Small Heat Shock Protein Studied by Peptide Mapping and Mass Spectrometry Using Purified Recombinant Protein From Arabidopsis Thaliana and Pea

  • Gustavsson N
  • Emanuelsson A
  • Härndahl U
  • et al.
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Abstract

Purified recombinant heat shock protein (HSP) 21 oligomer subjected to oxidative stress became resistant to methionine-specific CNBr-cleavage, which indicated that the methionine residues had been oxidized to methionine sulfoxides. The HSP 21 oligomer also exhibited a conformational change when it became oxidized, which was evident as a changed mobility and as an alteration in its tryptic digest peptide pattern

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Gustavsson, N., Emanuelsson, A., Härndahl, U., & Sundby, C. (1998). The Chloroplast Small Heat Shock Protein Studied by Peptide Mapping and Mass Spectrometry Using Purified Recombinant Protein From Arabidopsis Thaliana and Pea. In Photosynthesis: Mechanisms and Effects (pp. 2457–2460). Springer Netherlands. https://doi.org/10.1007/978-94-011-3953-3_575

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