Header menu link for other important links
The ant-pro reverse-turn motif. Structural features and conformational characteristics
V.H. Thorat, T.S. Ingole, K.N. Vijayadas, R.V. Nair, S.S. Kale, , H.C. Davis, P. Prabhakaran, R.G. Gonnade, R.L. GawadeShow More
Published in
Issue: 17
Pages: 3529 - 3542
This article details the characteristic conformational features of the Ant-Pro reverse turn - a folded pseudo β-turn motif that displays a closed nine-membered-ring hydrogen-bonded network involving just two amino acid residues, namely anthranilic acid (Ant; a constrained β-amino acid), and proline (Pro; a constrained α-amino acid). The results from the extensive investigation of ten crystal structures and their NMR conformations in the solution state provide a clear idea about the conformational characteristics of the Ant-Pro reverse turn. The Ant and Pro residues, which form the turn segment, maintain a perfect antiperiplanar orientation throughout, leaving little possibility for the formation of the otherwise possible six-membered hydrogen-bonding that requires a coplanar disposition of the two amino acid residues, as clearly evident from investigation of several crystal structures. The closed hydrogen-bonded network observed in the Ant-Pro reverse turn motif, formed in the forward direction of the sequence (1→2 amino acid interactions) involving only two amino acid residues, is in stark contrast to the native β-turns that involve four residues to form hydrogen-bonded network featuring backward 1←4 amino acid interactions. The readily available two-residue Ant-Pro motif raises the possibility of a practical utility, particularly in the application of rigidifying flexible peptide backbones by inserting the robust Ant-Pro reverse turn motifs into their backbone. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
About the journal
JournalEuropean Journal of Organic Chemistry