@article { ISI:000354199900018,
	title = {Role of N-terminal proline in stabilizing the Ant-Pro zipper motif},
	journal = {New Journal of Chemistry},
	volume = {39},
	number = {5},
	year = {2015},
	month = {MAR},
	pages = {3327-3332},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>Hetero-chiral hybrid peptides of the general sequence (L)alpha beta(D)(n)alpha beta(n) featuring proline (Pro, a constrained alpha-amino acid) and anthranilic acid (Ant, a constrained beta-amino acid) as building blocks, where n = 2, 4 etc., form a three-dimensional zipper-like architecture. These zipper peptides attain stable conformation by balancing the co-operative contribution of two competing non-covalent forces, namely hydrogen bonding and aromatic stacking. However, the selection of the N-terminal residue also stands to be one of the key contributors in stabilising the unusually long-range intramolecular hydrogen bond, featuring 26 atoms in the H-bonded ring observed at the termini. This article deals with the substitution alterations at the N-terminus of the zipper motif and their consequent influences on its structure and stability. In this study, the N-terminal Pro residue of the zipper motif was substituted with a flexible amino acid, alanine, and a constrained acyclic amino acid, 2-aminoisobutyric acid, to investigate the role of N-terminal proline in stabilizing the Ant-Pro zipper motif, and its stabilities were assessed by employing solution-state NMR and restrained MD simulation studies.</p>},
	issn = {1144-0546},
	doi = {10.1039/c4nj02151g},
	author = {Kheria, Sanjeev and Nair, Roshna V. and Kotmale, Amol S. and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
