Circular dichroism studies of the mitochondrial channel, VDAC, from Neurospora crassa.

@article{Shao1996CircularDS,
  title={Circular dichroism studies of the mitochondrial channel, VDAC, from Neurospora crassa.},
  author={Ling Shao and Kathleen W. Kinnally and Carmen A. Mannella},
  journal={Biophysical journal},
  year={1996},
  volume={71 2},
  pages={778-86}
}
The protein that forms the voltage-gated channel VDAC (or mitochondrial porin) has been purified from Neurospora crassa. At room temperature and pH 7, the circular dichoism (CD) spectrum of VDAC suspended in octyl beta-glucoside is similar to those of bacterial porins, consistent with a high beta-sheet content. When VDAC is reconstituted into phospholipid liposomes at pH 7, a similar CD spectrum is obtained and the liposomes are rendered permeable to sucrose. Heating VDAC in octyl beta… CONTINUE READING

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