Structure and potential C-terminal dimerization of a recombinant mutant of surfactant-associated protein C in chloroform/methanol.

@article{Luy2004StructureAP,
  title={Structure and potential C-terminal dimerization of a recombinant mutant of surfactant-associated protein C in chloroform/methanol.},
  author={Burkhard Luy and Alexander C. Diener and R. Hummel and Ernst Sturm and W. Ulrich and Christian Griesinger},
  journal={European journal of biochemistry},
  year={2004},
  volume={271 11},
  pages={
          2076-85
        }
}
The solution structure of a recombinant mutant [rSP-C (FFI)] of the human surfactant-associated protein C (hSP-C) in a mixture of chloroform and methanol was determined by high-resolution NMR spectroscopy. rSP-C (FFI) contains a helix from Phe5 to the C-terminal Leu34 and is thus longer by two residues than the helix of porcine SP-C (pSP-C), which is reported to start at Val7 in the same solvent. Two sets of resonances at the C-terminus of the peptide were observed, which are explained by low… CONTINUE READING

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