02114nas a2200157   4500008004100000022001400041245010800055210006900163260009600232300001400328490000700342520142700349100002501776700002601801856012901827       2006                        eng d  a0031-865500aBinding of T-antigen disaccharides to artocarpus hirsuta lectin and jacalin are energetically different0 aBinding of Tantigen disaccharides to artocarpus hirsuta lectin a  aBIOTECH PARK, 1021 15TH ST, SUITE 9, AUGUSTA, GA 30901-3158 USAbAMER SOC PHOTOBIOLOGYcSEP  a1315-13180 v823 a<p>The thermodynamics of binding of Me-alpha-GalNAc, Gal-beta-1-3GalNAc-alpha-O-Me (T-antigen-alpha), Gal-beta-1-3GalNAc and Gal-alpha-1-6Glc (mellibiose) to Artocarpus hirsuta lectin was studied using fluorescence spectroscopy. The binding affinities of the saccharides are in the order Gal-beta-1-3GalNAc-alpha-O-Me &gt; Me-alpha-GalNAc &gt; Me-alpha-Gal &gt; Gal-beta-1-3GalNAc &gt; Gal-alpha-1-6Glc. The binding affinities were comparable to those for jacalin. However, binding of the saccharides to the A. hirsuta lectin was not affected as strongly by temperature as observed in jacalin and the trend was found to be reversed. Values for Delta H and Delta S were found to be positive in A. hirsuta lectin-disaccharide binding despite similar binding affinities. Thus, with 99% structural and 96% sequence homology, with similar sugar specificity and affinity, the energetics of the disaccharide binding of the two lectins seem to be different. Me-alpha-GalNAc binding to A. hirsuta lectin is enthalpically driven, because the association constant decreases with increasing temperature. However, the binding of the T-antigen disaccharides and mellibiose disaccharides to the lectin is entropically driven. The difference in the molecular associations in the packing and variation of the C-terminal length of the P chain of the A. hirsuta lectin could be reflected in the different disaccharide binding energetics.</p>1 aGaikwad, Sushama, M.1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/binding-t-antigen-disaccharides-artocarpus-hirsuta-lectin-and-jacalin-are-energetically-002107nas a2200241   4500008004100000022001400041245014100055210006900196260008600265300001200351490000700363520118300370653001601553653002401569653001901593653001401612100001801626700001901644700002501663700002001688700002501708856013201733       2007                        eng d  a1521-654300aBile salt hydrolase, the member of Ntn-hydrolase family: differential modes of structural and functional transitions during denaturation0 aBile salt hydrolase the member of Ntnhydrolase family differenti  a325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USAbTAYLOR & FRANCIS INCcFEB  a118-1250 v593 a<p>Conformational transitions and functional stability of the bile salt hydrolase (BSH; cholylglycine EC: 3.5.1.24) from Bifidobacterium longum (BlBSH) cloned and expressed in E. coli were studied under thermal, chemical and pH-mediated denaturation conditions using fluorescence and CD spectroscopy. Thermal and Gdn-HCl-mediated denaturation of BlBSH is a multistep process of inactivation and unfolding. The inactivation and unfolding of the enzyme was found to be irreversible. Enzyme activity seems sensitive to even minor conformational changes at the active site. Thermal denaturation as such did not result in any insoluble protein aggregates. However, on treating with 0.25-1 M Gdn-HCl the enzyme showed increasing aggregation at temperatures of 40-55 degrees C indicating more complex structural changes taking place in the presence of chemical denaturants. The enzyme secondary structure was still intact at acidic pH (pH 1-3). The perturbation in the tertiary structure at the acidic pH was detected through freshly formed solvent exposed hydrophobic patches on the enzyme. These changes could be due to the formation of an acid-induced molten globule-like state.</p>10aAggregation10aBile salt hydrolase10amolten-globule10aUnfolding1 aKumar, Suresh1 aSuresh, C., G.1 aBrannigan, James, A.1 aDodson, Guy, G.1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/bile-salt-hydrolase-member-ntn-hydrolase-family-differential-modes-structural-and-functional