Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban.

@article{Ludlam1996FourierTI,
  title={Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban.},
  author={C F Ludlam and Isaiah T. Arkin and Xiang ming Liu and Miriam Rothman and Parshuram Rath and Saburo Aimoto and Steven Oliver Smith and Donald M. Engelman and Kenneth J Rothschild},
  journal={Biophysical journal},
  year={1996},
  volume={70 4},
  pages={1728-36}
}
Phospholamban is a 52-amino acid residue membrane protein that regulates Ca(2+)-ATPase activity in the sarcoplasmic reticulum of cardiac muscle cells. The hydrophobic C-terminal 28 amino acid fragment of phospholamban (hPLB) anchors the protein in the membrane and may form part of a Ca(2+)-selective ion channel. We have used polarized attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy along with site-directed isotope labeling to probe the local structure of hPLB. The… CONTINUE READING
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