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  • Title: Energetics of heterodimer formation among gramicidin analogues with an NH2-terminal addition or deletion. Consequences of missing a residue at the join in the channel.
    Author: Durkin JT, Providence LL, Koeppe RE, Andersen OS.
    Journal: J Mol Biol; 1993 Jun 20; 231(4):1102-21. PubMed ID: 7685829.
    Abstract:
    We examined the properties of membrane-spanning channels formed by gramicidin analogues that differ from [Val1]gramicidin A by having a single residue deletion or insertion at the formyl-NH terminus and of hybrid channels formed between such 14-, 15-, and 16-residue analogues. The channels' backbone structure, and helix sense, are not affected by the sequence modifications, because hybrid channels were observed for all combinations tested, and there was no excess energetic cost associated with hybrid channel formation. When hybrid channels form between analogues of different length the hybrid channel stability depends on the nature of the sequence dissimilarity. If two analogues differ by one residue (delta n = 1), the hybrid channels are destabilized by approximately 10 kJ/mol, because there is a defect (a "gap" in the peptide backbone) at the join between the two beta 6.3-helical monomers such that the dimer is stabilized by only five intermolecular C = O ... H-N hydrogen bonds rather than the usual six. This defect also alters the hybrid channels' permeability characteristics: the single-channel conductances are decreased, as if there were an additional barrier to ion movement through the channel. If the formyl-NH-terminal residue is Gly (and delta n = 1), the hybrid channels show multi-state behavior with voltage-dependent transitions between two conductance levels. If two analogues differ by two residues (delta n = 2), the hybrid channels are stabilized by 3 kJ/mol, indicating that structural continuity at the join between the monomers has been restored, as have the hybrid channels' permeability characteristics. The increased hybrid channel stability (when delta n = 2) may arise from altered membrane-channel interactions.
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