摘要: This article develops the possibility of using conformationally rigid peptides as bioorganic model systems. Stereochemical constraints on peptide backbone folding may be introduced by judicious use sequences containingα-aminoisobutyric acid and proline. The design synthetic models 310-helical β-turn conformations is reviewed. Attempts at generating antiparallelβ-sheet are discussed. disulphide crosslinks illustrated in application cystine to generate forβ-turn conformations. Using a well-defined skeleton attempts for protein binding sites examined. Helical retinylidene-lysine bacteriorhodopsin chromophore. Lysine containing chiral diamines explored model-binding bilirubin gossypol. An attempt active site loop redox protein, thioredoxin, described.
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