<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Gowda, Nagaraj M.</style></author><author><style face="normal" font="default" size="100%">Goswami, Usha</style></author><author><style face="normal" font="default" size="100%">Khan, Mohammad Islam</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)</style></title><secondary-title><style face="normal" font="default" size="100%">Fish &amp; Shellfish Immunology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Fluorescence spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Holothuria scabra</style></keyword><keyword><style  face="normal" font="default" size="100%">Lectin</style></keyword><keyword><style  face="normal" font="default" size="100%">marine invertebrate</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermodynamic properties</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><publisher><style face="normal" font="default" size="100%">ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">24-28 OVAL RD, LONDON NW1 7DX, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">24</style></volume><pages><style face="normal" font="default" size="100%">450-458</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A novel lectin was purified from the coelomic fluid of the sea cucumber Holothuria scabra (HSL), subjected to bacterial challenge. HSL is a monomeric glycoprotein of molecular mass 182 kDa. The lectin is highly thermostable as it retains full activity for 1 h at 80 degrees C. Further, the hemagglutination activity of HSL is unaffected by pH in the range 2-11. Unlike other lectins purified from marine invertebrates, the hemagglutination activity of HSL does not require any divalent metal ions. The affinity profile of HSL was studied by a combination of hemagglutination inhibition and fluorescence spectroscopy. HSL binds to desialylated glycoproteins, Me alpha Gal, T-antigen and T (alpha-ser)-antigen with a distinction between beta 1-4 and beta 1-3 linkages. Me alpha-T-antigen was a potent ligand having highest affinity (K-a 8.32 x 10(7) M-1). Monosaccharide binding is enthalphically driven while disaccharide binding involves both entropic and enthalpic contributions. (c) 2008 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.044</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sabale, Pramod M.</style></author><author><style face="normal" font="default" size="100%">Nuthanakanti, Ashok</style></author><author><style face="normal" font="default" size="100%">Srivatsan, Seergazhi G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Synthesis and fluorescence properties of a full set of extended RNA base analogues</style></title><secondary-title><style face="normal" font="default" size="100%">Indian Journal of Chemistry Section A-Inorganic Bio-Inorganic Physical Theoretical &amp; Analytical Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Environment sensitive probes</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescence probes</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescence spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Nucleic acids</style></keyword><keyword><style  face="normal" font="default" size="100%">Ribonucleoside analogues</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">8-9, SI</style></number><publisher><style face="normal" font="default" size="100%">NATL INST SCIENCE COMMUNICATION-NISCAIR</style></publisher><pub-location><style face="normal" font="default" size="100%">DR K S KRISHNAN MARG, PUSA CAMPUS, NEW DELHI 110 012, INDIA</style></pub-location><volume><style face="normal" font="default" size="100%">52</style></volume><pages><style face="normal" font="default" size="100%">1004-1013</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The synthesis and photophysical characterization of a complete set of fluorescent RNA base analogues derived by conjugating benzofuran moiety at the 5- and 8-positions of pyrimidine and purine bases, respectively, are described. Benzofuran-modified pyrimidine and purine ribonucleoside analogues exhibit Contrasting fluorescence properties. Pyrimidine analogues are moderately emissive with emission maximum in the visible region, and importantly, are highly sensitive to solvent polarity and Viscosity changes. On the other hand, purine analogues are highly emissive and are minimally affected by solvation. and viscosity effects. Thorough photophysical analysis reveals that the pyrimidine and purine ribonucleosides displaying distinct and-probe-like fluorescence properties could be useful in designing nucleic acid based biophysical tools to study nucleic acid structure and function.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">8-9</style></issue><custom3><style face="normal" font="default" size="100%">Indian</style></custom3><custom4><style face="normal" font="default" size="100%">0.628
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mishra, Prajna</style></author><author><style face="normal" font="default" size="100%">Patni, Divya</style></author><author><style face="normal" font="default" size="100%">Jha, Santosh Kumar</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">pH-dependent protein stability switch coupled to the perturbed pKa of a single ionizable residue</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">electrostatic interactions</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescence spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermodynamic stability</style></keyword><keyword><style  face="normal" font="default" size="100%">Unfolded proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">274</style></volume><pages><style face="normal" font="default" size="100%">106591</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The contribution of electrostatic interactions in protein stability has not been fully understood. Burial of an ionizable amino acid inside the hydrophobic protein core can affect its ionization equilibrium and shift its pKa differentially in the native (N) and unfolded (U) states of a protein and this coupling between the folding/ unfolding cycle and the ionization equilibria of the ionizable residue can substantially influence the protein stability. Here, we studied the coupling of the folding/unfolding cycle with the ionization of a buried ionizable residue in a multi-domain protein, Human Serum Albumin (HSA) using fluorescence spectroscopy. A pHdependent change in the stability of HSA was observed in the near native pH range (pH 6.0-9.0). The protonation-deprotonation equilibrium of a single thiol residue that is buried in the protein structure was identified to give rise to the pH-dependent protein stability. We quantified the pKa of the thiol residue in the N and the U states. The mean pKa of the thiol in the N state was upshifted by 0.5 units to 8.7 due to the burial of the thiol in the protein structure. Surprisingly, the mean pKa of the thiol in the U state was observed to be downshifted by 1.3 units to 6.9. These results indicate that some charged residues are spatially proximal to the thiol group in the U state. Our results suggest that, in addition to the N state, electrostatic interactions in the U state are important determinants of protein stability.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.352</style></custom4></record></records></xml>