Journal
EUROPEAN JOURNAL OF ORGANIC CHEMISTRY
Volume 2013, Issue 17, Pages 3529-3542Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/ejoc.201201739
Keywords
Peptides; Peptidomimetics; Protein structures; Protein folding
Categories
Funding
- Council of Scientific and Industrial Research (CSIR), New Delhi
- International Foundation for Science, Sweden
- NCL-IGIB (New Delhi)
Ask authors/readers for more resources
This article details the characteristic conformational features of the Ant-Pro reverse turn ? a folded pseudo -turn motif that displays a closed nine-membered-ring hydrogen-bonded network involving just two amino acid residues, namely anthranilic acid (Ant; a constrained -amino acid), and proline (Pro; a constrained -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 (12 amino acid interactions) involving only two amino acid residues, is in stark contrast to the native -turns that involve four residues to form hydrogen-bonded network featuring backward 14 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available