01551nas a2200193   4500008004100000245007200041210006700113260000800180300001400188490000700202520089000209100002401099700002201123700002301145700002401168700003501192700002801227856010201255       2016                        eng d00a3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides0 a3Aminothiophenecarboxylic acid 3Atcinduced folding in peptides  cSEP  a9205-92100 v403 aThis 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.1 aIngole, Tukaram, S.1 aKotmale, Amol, S.1 aGawade, Rupesh, L.1 aGonnade, Rajesh, G.1 aRajamohanan, Pattuparambil, R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/3-aminothiophenecarboxylic-acid-3-atc-induced-folding-peptides