01208nas a2200205   4500008004100000022001400041245007200055210006900127260011000196300001400306490000600320520041000326100002300736700003300759700002400792700002300816700003500839700002800874856010000902       2011                        eng d  a1477-052000aConcurrent display of both alpha- and beta-turns in a model peptide0 aConcurrent display of both alpha and betaturns in a model peptid  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcMAY  a5762-57650 v93 a<p>This article describes a model peptide that concurrently displays both alpha- and beta-turns, as demonstrated by structural investigations using single crystal X-ray crystallography and solution-state NMR studies. The motif reported herein has the potential for the design of novel conformationally ordered synthetic oligomers with structural architectures distinct from those classically observed.</p>1 aSrinivas, Deekonda1 aVijayadas, Kuruppanthara, N.1 aGonnade, Rajesh, G.1 aPhalgune, Usha, D.1 aRajamohanan, Pattuparambil, R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/concurrent-display-both-alpha-and-beta-turns-model-peptide-001228nas a2200205   4500008004100000022001400041245008900055210006900144260011000213300001400323490000700337520040000344100001700744700002200761700003100783700002600814700003500840700002800875856011900903       2015                        eng d  a1477-052000aConformational modulation of peptides using beta-amino benzenesulfonic acid ((S)Ant)0 aConformational modulation of peptides using betaamino benzenesul  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcDEC  a2087-20910 v133 a<p>This communication describes the utility of a conformationally restricted aromatic beta-amino acid (2-aminobenzenesulfonic acid, (S)Ant) inducing various folding interactions in short peptides. Sandwiching (S)Ant between diverse amino acid residues was shown to form robust folded architectures featuring a variety of H-bonded networks, suggesting its utility in inducing peptide folding.</p>1 aPriya, Gowri1 aKotmale, Amol, S.1 aChakravarty, Debamitra, K.1 aPuranik, Vedavati, G.1 aRajamohanan, Pattuparambil, R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/conformational-modulation-peptides-using-beta-amino-benzenesulfonic-acid-sant-001921nas a2200193   4500008004100000245008100041210006900122260000800191300001600199490000700215520124900222100002101471700001901492700002701511700002601538700003501564700001701599856011101616       2017                        eng d00aCucurbit[7]uril induced formation of fret-enabled unilamellar lipid vesicles0 aCucurbit7uril induced formation of fretenabled unilamellar lipid  cOCT  a10989-109990 v333 aA unique fluorescence resonance energy transfer (FRET) process is found to be operational in a unilamellar lipid self-assembly in the aqueous phase. A newly synthesized naphthyl based long chain lipid derivative [N-(naphthalene-1-ylmethyl)tetradecane-1-ammonium chloride, 14NA(+)] forms various self-assembled architectures in the aqueous phase. Controlled changes in lipid concentration lead to a transition of the self-assemblies from micelles to vesicles to rods. In the presence of cucurbit[7]uril (CB7), 14NA(+) forms a host-guest [2]pseudorotaxane complex (CB7(sic)14NA(+)) and secondary interactions lead to the formation of a lipid bilayer with hydrophobic pockets situated in between the layers. The change in the structure of 14NA(+) assemblies, interaction with CB7 and formation of supramolecular assemblies of CB7(sic)14NA(+) were examined using light scattering, spectroscopic, and microscopic techniques. Entrapment of a luminescent dye, anthracene within the hydrophobic bilayer of the supramolecular assembly CB7(sic)14NA(+) favors a modified luminescent response due to an efficient FRET process. Further, the FRET process could be controlled by thermal and chemical stimuli that induce transformation of unilamellar vesicles.1 aKushwaha, Shilpi1 aMaity, Arunava1 aGangopadhyay, Monalisa1 aRavindranathan, Sapna1 aRajamohanan, Pattuparambil, R.1 aDas, Amitava  uhttps://library.ncl.res.in/content/cucurbit7uril-induced-formation-fret-enabled-unilamellar-lipid-vesicles01323nas a2200205   4500008004100000245010100041210006900142260000800211300001400219490000700233520057900240100002200819700001900841700002400860700001900884700001900903700003500922700002800957856013200985       2018                        eng d00aConformational studies of Ant-Pro motif-incorporated cyclic peptides: gramicidin S and avellanin0 aConformational studies of AntPro motifincorporated cyclic peptid  cJAN  a1197-12010 v423 aThis paper reports conformational changes observed in cyclic bioactive peptides such as gramicidin S and avellanin upon incorporation of a pseudo-beta (C9) Ant-(D)Pro turn motif in their structural frameworks. Solution-state studies suggested that a synthetic gramicidin S analog exhibits a beta-sheet conformation with C9 and C17 intramolecular hydrogen bonding patterns, while its truncated analog disturbs the beta-sheet conformation. Structural details were obtained using a combination of CD studies, X-ray crystal structure studies and nOe-based MD simulation studies.1 aKotmale, Amol, S.1 aSangtani, Ekta1 aGonnade, Rajesh, G.1 aSarkar, Dhiman1 aBurade, Sachin1 aRajamohanan, Pattuparambil, R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/conformational-studies-ant-pro-motif-incorporated-cyclic-peptides-gramicidin-s-and-avellanin