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. 1982 Jan;37(1):319–328. doi: 10.1016/S0006-3495(82)84680-8

High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface.

L R Brown, W Braun, A Kumar, K Wüthrich
PMCID: PMC1329145  PMID: 6275926

Abstract

Previously, the size and stoichiometry of mixed micelles of perdeuterated dodecylphosphocholine and melittin were characterized and the 1H NMR spin systems of most amino acid residues of micelle-bound melittin identified. One- and two-dimensional 1H-1H Overhauser experiments have now been used to obtain qualitative information on intramolecular proton-proton distances. These data show that the N-terminal and the C-terminal segments of melittin form two spatially distinct, compact domains; using lipid spin labels these could be located near the micelle surface. For the C-terminal domain a detailed conformation was determined by using the distance contraints from the Overhauser studies as input for a distance geometry algorithm.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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