Folding of apominimyoglobin.

@article{Sanctis1994FoldingOA,
  title={Folding of apominimyoglobin.},
  author={Giampiero de Sanctis and Franca Ascoli and Maurizio Brunori},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 24},
  pages={11507-11}
}
The acid unfolding pathway of apominimyoglobin (apo-mini-Mb), a 108-aa fragment (aa 32-139) of horse heart apomyoglobin has been studied by means of circular dichroism, in comparison with the native apoprotein. Similar to sperm whale apomyoglobin [Hughson, F. M., Wright, P. E. & Baldwin, R. L. (1990) Science 249, 1544-1548], a partly folded intermediate (alpha-helical content approximately 35%) is populated at pH 4.2 for horse heart apomyoglobin. For this intermediate, Hughson et al. proposed a… CONTINUE READING

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