Conformational perturbations in retro‐analogs of the tBuCO‐Ala‐Gly‐NHiPr dipeptide Crystal structure of the retro‐dipeptide with a reversed Ala‐Gly amide bond

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Abstract
The three retro-analogs of the tBuCo-Ala-Gly-NHiPr dipeptide, in which each amide bond had been successively reversed, were studied in solution by 1H-n.m.r. and i.r. spectroscopy with reference to conformational properties of their parent dipeptide. Reversal of the Ala-Gly amide bond proved to perturb the folding tendenyx of the backbone less than the inversion of either of the terminal amide bonds. The crystal structure of the retro-peptide containing a reversed Ala-Gly amide bond was also solved by X-ray diffraction and constitutes the first available data for this retro-peptide series. In contrast to the .beta.II-folded structure of the parent dipeptide, the retro-peptide molecule adopts an open conformation in the crystal.

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