@article { ISI:000315168800015,
	title = {Orthanilic acid-promoted reverse turn formation in peptides},
	journal = {Chemical Communications},
	volume = {49},
	number = {22},
	year = {2013},
	month = {JAN},
	pages = {2222-2224},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>Orthanilic acid (2-aminobenzenesulfonic acid, (S)Ant), an aromatic beta-amino acid, has been shown to be highly useful in inducing a folded conformation in peptides. When incorporated into peptide sequences (Xaa-(S)Ant-Yaa), this rigid aromatic beta-amino acid strongly imparts a reverse-turn conformation to the peptide backbone, featuring robust 11-membered-ring hydrogen-bonding.</p>},
	issn = {1359-7345},
	doi = {10.1039/c3cc40522b},
	author = {Kale, Sangram S. and Priya, Gowri and Kotmale, Amol S. and Gawade, Rupesh L. and Puranik, Vedavati G. and Rajamohanan, P. R. and Sanjayan, Gangadhar J.}
}
