Conformational and aggregational states of omega-aminoacylmelittin derivatives.

@article{Ramalingam1993ConformationalAA,
  title={Conformational and aggregational states of omega-aminoacylmelittin derivatives.},
  author={K. Ramalingam and J. Bello},
  journal={Biochemistry},
  year={1993},
  volume={32 1},
  pages={
          253-9
        }
}
  • K. Ramalingam, J. Bello
  • Published 1993
  • Chemistry, Medicine
  • Biochemistry
  • Melittin, a 26-residue peptide from bee venom, is known to change from a largely random to a largely alpha-helical conformation as a function of peptide concentration, pH, and ionic strength. In this report, we have determined the effect of displacing the positive charges of the amino groups of N-terminal glycine and lysine residues away from the backbone of melittin in coil-to-helix transitions by using omega-aminoacyl derivatives of melittin. These were prepared by acylating the amino groups… CONTINUE READING
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