@article { ISI:000331895900018,
	title = {Conformational modulation of peptide secondary structures using beta-aminobenzenesulfonic acid},
	journal = {Chemical Communications},
	volume = {50},
	number = {22},
	year = {2014},
	month = {JAN},
	pages = {2886-2888},
	publisher = {ROYAL SOC CHEMISTRY},
	type = {Article},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>This communication describes the influence of beta-aminobenzenesulfonic acid ((S)Ant) on the conformational preferences of hetero foldamers. The designed (Aib-(S)Ant-Aib)(n) and (Aib-(S)Ant-Pro)(n) oligomers display a well-defined folded conformation featuring intramolecular mixed hydrogen bonding (7/11) and intra-residual (6/5) H-bonding interactions, respectively.</p>},
	issn = {1359-7345},
	doi = {10.1039/c3cc48850k},
	author = {Kale, Sangram S. and Kunjir, Shrikant M. and Gawade, Rupesh L. and Puranik, Vedavati G. and Rajamohanan, P. R. and Sanjayan, Gangadhar J.}
}
