• DOI:10.1016/0014-5793(91)81417-7
Corpus ID: 30227820

Conformational changes in melittin upon complexation with an anionic melittin analog

@article{Ramalingam1991ConformationalCI,
  title={Conformational changes in melittin upon complexation with an anionic melittin analog},
  author={K. Ramalingam and J. Bello and S. Aimoto},
  journal={FEBS Letters},
  year={1991},
  volume={295}
}

K. Ramalingam, J. Bello, S. Aimoto

Published 1991

Chemistry, Medicine

FEBS Letters

Melittin and its Glu‐(7,21,22,23,24) analog upon mixing in equimolar concentrations form a hybrid oligomer with significant helical structure, in conditions in which each peptide separately adopts a largely disordered structure. The hybrid exhibits both cold‐ and heat‐induced denaturations similar to the phenomena exhibited by proteins. The hybrid also retains significant residual structure at higher temperature, similar to the ‘molten globular state’ that has been suggested for proteins… CONTINUE READING

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