Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy.

@article{Gordon2000ConformationalMO,
  title={Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy.},
  author={Larry M. Gordon and Ka Yee C Lee and M. Michael Quincy Lipp and Joseph A Zasadzinski and Frans J Walther and Mark Sherman and Anthony J. Waring},
  journal={The journal of peptide research : official journal of the American Peptide Society},
  year={2000},
  volume={55 4},
  pages={
          330-47
        }
}
Synthetic peptides based on the N-terminal domain of human surfactant protein B (SP-B1-25; 25 amino acid residues; NH2-FPIPLPYCWLCRALIKRIQAMIPKG) retain important lung activities of the full-length, 79-residue protein. Here, we used physical techniques to examine the secondary conformation of SP-B1-25 in aqueous, lipid and structure-promoting environments. Circular dichroism and conventional, 12C-Fourier transform infrared (FTIR) spectroscopy each indicated a predominate alpha-helical… CONTINUE READING
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