@article { ISI:000320036300013,
	title = {Ant-pro reverse-turn motif. structural features and conformational characteristics},
	journal = {European Journal of Organic Chemistry},
	number = {17, SI},
	year = {2013},
	month = {JUN},
	pages = {3529-3542},
	publisher = {WILEY-V C H VERLAG GMBH},
	address = {BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANY},
	abstract = {<p>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.</p>},
	keywords = {Peptides, Peptidomimetics, Protein folding, Protein structures},
	issn = {1434-193X},
	doi = {10.1002/ejoc.201201739},
	author = {Thorat, Vijaykumar H. and Ingole, Tukaram S. and Vijayadas, Kuruppanthara N. and Nair, Roshna V. and Kale, Sangram S. and Ramesh, Veera V. E. and Davis, Hilda C. and Prabhakaran, Panchami and Gonnade, Rajesh G. and Gawade, Rupesh L. and Puranik, Vedavati G. and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
@article { ISI:000345826600002,
	title = {Heterogeneous foldamers from aliphatic-aromatic amino acid building blocks: current trends and future prospects},
	journal = {European Journal of Organic Chemistry},
	volume = {46},
	number = {35},
	year = {2014},
	month = {DEC},
	pages = {7763-7780},
	publisher = {WILEY-V C H VERLAG GMBH},
	address = {BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANY},
	abstract = {<p>Chemists{\textquoteright} constant pursuit of understanding of the underlying principles of nature{\textquoteright}s most intricate phenomenon such as protein folding has led to the development of the field of foldamers. The emergence of diverse classes of unnatural amino acid building blocks has unleashed countless opportunities to design, develop and explore the structural and functional aspects of synthetic peptides. One current trend in foldamer chemistry is the heterofoldamer approach, which involves systematic stoichiometric variation of various natural/unnatural amino acid residues, leading to conformational ordering with intriguing structural architectures. In this regard, the incorporation of aromatic amino acids provides efficient structural rigidification and tunability to the molecular scaffolds, which can exhibit a range of secondary structural features. Recent times have witnessed an upsurge of foldamers featuring aliphatic-aromatic residues with diverse structural propensities. This review is an effort to cover this rapidly developing field of foldamer science and also to envisage its future perspectives.</p>},
	keywords = {Amino acids, Conformation analysis, Foldamers, hydrogen bonding, Peptides, Stacking interactions},
	issn = {1434-193X},
	doi = {10.1002/ejoc.201402877},
	author = {Nair, Roshna V. and Vijayadas, Kuruppanthara N. and Roy, Arup and Sanjayan, Gangadhar J.}
}
