Conformational studies of anionic melittin analogues: Effect of peptide concentration, pH, ionic strength, and temperature—models for protein folding and halophilic proteins

@article{Ramalingam1992ConformationalSO,
  title={Conformational studies of anionic melittin analogues: Effect of peptide concentration, pH, ionic strength, and temperature—models for protein folding and halophilic proteins},
  author={K. Ramalingam and S. Aimoto and J. Bello},
  journal={Biopolymers},
  year={1992},
  volume={32}
}
  • K. Ramalingam, S. Aimoto, J. Bello
  • Published 1992
  • Chemistry, Medicine
  • Biopolymers
  • Melittin (MLT), a 26‐residue cationic (net charge +5 at pH 7.2) peptide from bee venom, is well known to be a monomeric, approximately random coil; but when its charges are reduced by titration, by acetylation (net charge +2) or succinylation (net charge −2), or by screening by salt, it goes over to tetrameric α‐helix. The conversion is promoted by raising the peptide concentration. The tetramer is held together by hydrophobia forces. We have changed the net charge to −6 by acylation with… CONTINUE READING
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