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- W2015384484 abstract "The recently isolated trichogin GA IV is a 10 amino acid, Aib-rich peptide with potent membrane-modifying properties. The peptide is too short to span lipid bilayers, so the mechanism by which trichogin GA IV interacts with biological membranes is unknown. The crystal structure has been solved, but there is much less information on the peptide's conformation in solution. This problem is addressed by examining the electron spin resonance (ESR) of single and double TOAC-labeled trichogin GA IV analogues, where TOAC is a rigid nitroxide amino acid and serves as an Aib analogue. The doubly labeled peptides, trich-1,4, -4,8 and -1,8, represent all possible trichogin GA IV analogues containing two Aib → TOAC substitutions. ESR in MeOH at 200 K of the g ≈ 2 spectral region suggests that the N-terminus from residues one through four adopts a helical structure similar to that observed in the crystal. However, the central and C-terminal regions appear to be structurally heterogeneous. To further resolve the solutio..." @default.
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- W2015384484 date "1999-07-01" @default.
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- W2015384484 title "Solution Structures of TOAC-Labeled Trichogin GA IV Peptides from Allowed (g ≈ 2) and Half-Field Electron Spin Resonance" @default.
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- W2015384484 doi "https://doi.org/10.1021/ja984255c" @default.
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