01978nas a2200193   4500008004100000022001400041245007100055210006900126260011000195300001400305490000700319520123400326100002001560700002101580700002201601700003501623700002801658856009801686       2015                        eng d  a1144-054600aRole of N-terminal proline in stabilizing the Ant-Pro zipper motif0 aRole of Nterminal proline in stabilizing the AntPro zipper motif  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcMAR  a3327-33320 v393 a<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>1 aKheria, Sanjeev1 aNair, Roshna, V.1 aKotmale, Amol, S.1 aRajamohanan, Pattuparambil, R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/role-n-terminal-proline-stabilizing-ant-pro-zipper-motif-0