Is the manganese stabilizing 33 kDa protein of photosystem II attaining a ‘natively unfolded’ or ‘molten globule’ structure in solution?

@article{Shutova2000IsTM,
  title={Is the manganese stabilizing 33 kDa protein of photosystem II attaining a ‘natively unfolded’ or ‘molten globule’ structure in solution?},
  author={T. Shutova and K. Irrgang and V. Klimov and G. Renger},
  journal={FEBS Letters},
  year={2000},
  volume={467}
}
  • T. Shutova, K. Irrgang, +1 author G. Renger
  • Published 2000
  • Chemistry, Medicine
  • FEBS Letters
    • This study compares the properties of the extrinsic 33 kDa subunit acting as ‘manganese stabilizing protein’ (MSP) of the water oxidizing complex with characteristic features of proteins that are known to attain a ‘natively unfolded’ or a ‘molten globule’ structure. The analysis leads to the conclusion that the MSP in solution is most likely a ‘molten globule’ with well defined compact regions of β structure. The possible role of these structural peculiarities of MSP in solution for its… CONTINUE READING
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      References

      SHOWING 1-10 OF 44 REFERENCES
      Secondary structure of the 33 kDa, extrinsic protein of Photosystem II: a far-UV circular dichroism study.
      • 52
      Manganese stabilizing protein of photosystem II is a thermostable, natively unfolded polypeptide.
      • 80
      Molten globule versus variety of intermediates: influence of anions on pH‐denatured apomyoglobin
      • 21
      Analysis of pH-induced structural changes of the isolated extrinsic 33 kilodalton protein of photosystem II.
      • 65
      Structural basis of the stability of a lysozyme molten globule
      • 111
      Packing interactions in the apomyglobin folding intermediate
      • 147
      Leucine 245 is a critical residue for folding and function of the manganese stabilizing protein of photosystem II.
      • 31
      Extrinsic 33-kilodalton protein of spinach oxygen-evolving complexes: kinetic studies of folding and disulfide reduction.
      • 40
      A native tertiary interaction stabilizes the A state of cytochrome c.
      • 80
      Acid-induced folding of proteins.
      • 460
      • PDF