@article { ISI:000297737900020,
	title = {Synthesis and structural characterization of homochiral homo-oligomers of parent CIS- and trans-furanoid-beta-amino acids},
	journal = {Chemistry-A European Journal},
	volume = {17},
	number = {46},
	year = {2011},
	month = {NOV},
	pages = {12946-12954},
	publisher = {WILEY-V C H VERLAG GMBH},
	address = {PO BOX 10 11 61, D-69451 WEINHEIM, GERMANY},
	abstract = {<p>The synthesis of homochiral homo-oligomers of cis- and trans-3-aminotetrahydrofuran-2-carboxylic acids (parent cis- and trans-furanoid-beta-amino acids, referred to as {\textquoteleft}{\textquoteleft}cis-/trans-FAA{\textquoteright}{\textquoteright}) has been carried out to understand their secondary structures and their dependence on the ring heteroatom. The oligomers of two diastereomers have been shown to have a distinct left-handed helicity. The cis-FAA homo-oligomers show a 14-helix structure, in contrast to the homo-oligomers of cis-ACPC, which adopt a sheet like structure. The trans-FAA homo-oligomers were found to adopt a 12-helix structure, the same trend found in trans-ACPC homo-oligomers. With the help of ab initio calculations, the structural features of cis-ACPC and cis-FAA hexamers were compared. We believe that the more compact packing of the cis-FAA hexapeptide should be due to a more favorable interaction between the ring and the backbone amide hydrogen.</p>},
	keywords = {ab initio calculations, Amino acids, Density functional calculations, Peptides, secondary structures},
	issn = {0947-6539},
	doi = {10.1002/chem.201101855},
	author = {Pandey, Sunil K. and Jogdand, Ganesh F. and Oliveira, Joao C. A. and Mata, Ricardo A. and Rajamohanan, Pattuparambil R. and Ramana, Chepuri V.}
}
@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.}
}
