Nicolas Mandard , Henri Labbé , Pedro Da Silva , Charles Hetru , Céline Landon , Françoise Vovelle
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Abstract
Androctonin is a 25-residue antibacterial peptide extracted from the hemolymph of the scorpion Androctonus australis. In order to understand the structural requirements for hairpin fold and for interactions with the bacterial membrane, we have analysed the chemical shifts and the nOes of three synthetic androctonin mutants for which the disulfide bridges were selectively removed.
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