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Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.
Structures in four different crystal forms of [Leu1]zervamicin, a membrane channel-forming polypeptide from Emericellopsis salmosynnemata, have been determined by x-ray diffraction, suggesting a gating mechanism for cation transport. Expand
Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment.
Crystals of an ion-channel-forming peptaibol peptide in a partial membrane environment have been obtained by cocrystallizing antiamoebin with n-octanol. The antiamoebin molecule has a bent helicalExpand
The design and synthesis of redox core-alpha amino acid composites based on thiol-disulfide exchange mechanism and a comparative study of their zinc abstraction potential from [CCXX] boxes in proteins
The design and synthesis of agents that can abstract zinc from their [CCXX] (C=cysteine; X=cysteine/histidine) boxes by thioldisulfide exchange-having as control, the redox parities of the coreExpand
Conformation of valinomycin in a triclinic crystal form.
  • I. Karle
  • Chemistry, Medicine
  • Journal of the American Chemical Society
  • 23 July 1975
Conformation of the flexible bent helix of Leu1‐zervamicin in crystal C and a possible gating action for ion passage
In the present crystal C there appears to be an additional conformation for the Gln (11) side chain (with ≈ 20% occupancy) that opens the channel for possible ion passage, which is quite similar to the conformations found in crystals A and B. Expand