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
    Structural basis of the stability of a lysozyme molten globule
    • 111
    Packing interactions in the apomyglobin folding intermediate
    • 147
    Acid-induced folding of proteins.
    • 460
    • PDF