@article { ISI:000372848000021,
	title = {Disruption of native beta-turns: consequence of folding competition between native and orthanilic acid proline-based pseudo beta-turn},
	journal = {European Journal of Organic Chemistry},
	number = {7},
	year = {2016},
	month = {MAR},
	pages = {1380-1388},
	publisher = {WILEY-V C H VERLAG GMBH},
	address = {POSTFACH 101161, 69451 WEINHEIM, GERMANY},
	abstract = {<p>Five tetrapeptides comprising beta-turn-forming elements and a pseudo beta-turn (C9 H-bonding) based on an SAntPro (orthanilic acid - proline) motif were designed and synthesized. Their extensive conformational investigation by single-crystal X-ray crystallography, solution-state 2D NMR spectroscopic, and nOe-restrained MD simulation studies revealed the formation of C14 or C9 folding and disruption of the native beta-turn (C10 H-bonding) architecture. The striking difference between the psi(psi(2)) angle of {\textquoteleft}{\textquoteleft}i + 2{\textquoteright}{\textquoteright} residues of native beta-turn and designed peptides suggest that formation of the native beta-turn is not favored. The results suggest that other turn-forming motifs can dramatically modulate the stability of the native beta-turn structure.</p>},
	keywords = {Conformation analysis, hydrogen bonds, Peptidomimetics, structure elucidation},
	issn = {1434-193X},
	doi = {10.1002/ejoc.201501558},
	author = {Ingole, Tukaram S. and Vijayadas, Kuruppanthara N. and Chaitanya, K. N. and Kotmale, Amol S. and Gawade, Rupesh L. and Gonnade, Rajesh G. and Rajamohanan, P. R. and Sanjayan, Gangadhar J.}
}
