02180nas a2200205   4500008004100000022001400041245018700055210006900242260007500311300001200386490000700398520133500405653000801740653001401748653002801762653002001790100002101810700001401831856012901845       2009                        eng d  a1053-050900aFluorescence study on interactions of alpha-crystallin with the molten globule state of 1, 4-beta-D-glucan glucanohydrolase from thermomonospora sp induced by guanidine hydrochloride0 aFluorescence study on interactions of alphacrystallin with the m  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGER/PLENUM PUBLISHERScNOV  a967-9730 v193 a<p>In this paper, the interaction between alpha- crystallin and molten globule structure of 1,4-beta-D-Glucan Glucohydrolase (TSC) from an alkalothermophilic Thermomonospora sp. was investigated mainly by fluorescence quenching spectra, circular dichroism and three dimensional fluorescence spectra under simulative physiological conditions. Denaturation studies using GdnCl indicated that TSC folds through a partially folded state that resembles molten globule at 1.8 M GdnCl. The chaperone activity of alpha- crystallin was employed to study refolding of TSC. Here we studied the refolding of GdnCl denatured TSC from its molten globule state (TSC-m complex) in the presence and absence of alpha-crystallin to elucidate the molecular mechanism of chaperone-mediated in vitro folding. Our results, based on intrinsic tryptophan fluorescence and ANS binding studies, suggest that alpha-crystallin formed a complex with a putative intermediate molten globule - like intermediate in the refolding pathway of TSC. Reconstitution of the active TSC was observed on cooling the alpha-crystallin aEuro cent TSC -m complex to 4A degrees C. Addition of alpha-crystallin to the molten globule - like intermediate of TSC (TSC-m complex) complex initiated the refolding of TSC with 69 % recovery of the biological activity of the enzyme.</p>10aANS10aCellulase10aGuanidine hydrochloride10aProtein folding1 aJagtap, Sharmili1 aRao, Mala  uhttps://library.ncl.res.in/content/fluorescence-study-interactions-alpha-crystallin-molten-globule-state-1-4-beta-d-glucan-002655nas a2200325   4500008004100000022001400041245008700055210006900142260007700211300001400288520149300302653001301795653002001808653002001828653002301848100002701871700002401898700003301922700002101955700002201976700002501998700002102023700002602044700002402070700002302094700002602117700003502143700002802178856012302206       2013                        eng d  a1434-193X00aAnt-pro reverse-turn motif. structural features and conformational characteristics0 aAntpro reverseturn motif structural features and conformational   aBOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANYbWILEY-V C H VERLAG GMBHcJUN  a3529-35423 a<p>This article details the characteristic conformational features of the Ant-Pro reverse turn ? a folded pseudo -turn motif that displays a closed nine-membered-ring hydrogen-bonded network involving just two amino acid residues, namely anthranilic acid (Ant; a constrained -amino acid), and proline (Pro; a constrained -amino acid). The results from the extensive investigation of ten crystal structures and their NMR conformations in the solution state provide a clear idea about the conformational characteristics of the Ant-Pro reverse turn. The Ant and Pro residues, which form the turn segment, maintain a perfect antiperiplanar orientation throughout, leaving little possibility for the formation of the otherwise possible six-membered hydrogen-bonding that requires a coplanar disposition of the two amino acid residues, as clearly evident from investigation of several crystal structures. The closed hydrogen-bonded network observed in the Ant-Pro reverse turn motif, formed in the forward direction of the sequence (12 amino acid interactions) involving only two amino acid residues, is in stark contrast to the native -turns that involve four residues to form hydrogen-bonded network featuring backward 14 amino acid interactions. The readily available two-residue Ant-Pro motif raises the possibility of a practical utility, particularly in the application of rigidifying flexible peptide backbones by inserting the robust Ant-Pro reverse turn motifs into their backbone.</p>10aPeptides10aPeptidomimetics10aProtein folding10aProtein structures1 aThorat, Vijaykumar, H.1 aIngole, Tukaram, S.1 aVijayadas, Kuruppanthara, N.1 aNair, Roshna, V.1 aKale, Sangram, S.1 aRamesh, Veera, V. E.1 aDavis, Hilda, C.1 aPrabhakaran, Panchami1 aGonnade, Rajesh, G.1 aGawade, Rupesh, L.1 aPuranik, Vedavati, G.1 aRajamohanan, Pattuparambil, R.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/ant-pro-reverse-turn-motif-structural-features-and-conformational-characteristics-0