@article {43630,
	title = {3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides},
	journal = {New Journal of Chemistry},
	volume = {40},
	year = {2016},
	month = {SEP},
	pages = {9205-9210},
	abstract = {This paper describes the consequences of incorporating a constrained heterocyclic aromatic b-amino acid 3-aminothiophenecarboxylic acid (3-Atc) into peptides containing beta-turn forming elements such as Pro-Gly motif and the effect on the secondary structural architecture of the entire peptide backbone. Conformational investigations of oligomers comprising an alpha,beta,alpha peptide sequence were carried out by single-crystal X-ray diffraction, solution-state NMR, nOe-restrained MD simulation and circular dichroism studies. The results suggested that these peptide sequences assume helical architecture. The helical folding in the oligomers was found to be devoid of inter-residual H-bonding, instead found to be stabilized by a co-operative effect of 6-membered H-bonding within the 3-Atc unit and conformational restrictions of individual amino acids in the peptide backbone.},
	doi = {10.1039/c6nj01667g},
	author = {Ingole, Tukaram S. and Kotmale, Amol S. and Gawade, Rupesh L. and Gonnade, Rajesh G. and Rajamohanan, Pattuparambil R. and Sanjayan, Gangadhar J.}
}
