Citation
Song, B., Bomar, M. G., Kibler, P., Kodukula, K., & Galande, A. K. (2012). The serine-proline turn: A novel hydrogen-bonded template for designing peptidomimetics. Organic letters, 14(3), 732-735.
Abstract
Serine-Proline (SP) dipeptide motifs have been shown to form unique hydrogen-bonding patterns in protein crystal structures. Peptides were designed to mimic these patterns by forming the 6 + 10 and the 9 + 10 hydrogen-bonded rings. Factors that contribute to the formation of SP turns include controlling backbone flexibility and amino acid chirality along with creating a hydrophobic environment around the intramolecular hydrogen bonds.
