<?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%">Dharker, Poorva N.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author><author><style face="normal" font="default" size="100%">Suresh, C. G.</style></author><author><style face="normal" font="default" size="100%">Dhuna, Vikram</style></author><author><style face="normal" font="default" size="100%">Khan, Mohammad Islam</style></author><author><style face="normal" font="default" size="100%">Singh, Jatinder</style></author><author><style face="normal" font="default" size="100%">Kamboj, Sukhdev Singh</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comparative studies of two araceous lectins by steady state and time-resolved fluorescence and CD spectroscopy</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Fluorescence</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Araceae lectins</style></keyword><keyword><style  face="normal" font="default" size="100%">Denaturation</style></keyword><keyword><style  face="normal" font="default" size="100%">fluorescence</style></keyword><keyword><style  face="normal" font="default" size="100%">Lifetime spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Secondary structure</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER/PLENUM PUBLISHERS</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING ST, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">19</style></volume><pages><style face="normal" font="default" size="100%">239-248</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Transitions in the tryptophan microenvironment and secondary structure of two monocot lectins from Sauromatum guttatum and Arisaema tortuosum under different denaturing conditions were studied by steady state and time resolved fluorescence and CD spectroscopy. The lectins exist as tetramers with a single tryptophan residue estimated per monomer, present in a polar environment. Quenching with ionic quenchers showed predominantly electropositive environment for tryptophan residues. Acrylamide had maximum quenching effect. A decrease in KI quenching due to lectin denaturation indicated redistribution of charges as a result of possible conformational change. The two values for lifetimes of tryptophanyl population (1.2-1.4 and 6.3-6.4 ns) reduced substantially on quenching or denaturation. Similarly, both the lectins showed a drastic loss of secondary structure in 5 M Gdn-HCl or 6 M Urea or at pH 2.0 and below. For the first time araceous lectins, like legume lectins are shown to bind adenine. The presence of a compact structure at alkaline pH 10.0-12.0 was observed in CD spectra.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.966</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%">Sharma, Urvashi</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author><author><style face="normal" font="default" size="100%">Suresh, C. G.</style></author><author><style face="normal" font="default" size="100%">Dhuna, Vikram</style></author><author><style face="normal" font="default" size="100%">Singh, Jatinder</style></author><author><style face="normal" font="default" size="100%">Kamboj, Sukhdev Singh</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Conformational transitions in ariesaema curvatum lectin: characterization of an acid induced active molten globule</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Fluorescence</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Araceae</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescence lifetime</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemagglutinin</style></keyword><keyword><style  face="normal" font="default" size="100%">Molten globule</style></keyword><keyword><style  face="normal" font="default" size="100%">Secondary structure</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermostability</style></keyword><keyword><style  face="normal" font="default" size="100%">Unfolding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER/PLENUM PUBLISHERS</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING ST, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">21</style></volume><pages><style face="normal" font="default" size="100%">753-763</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Biophysical characterization of a lectin from Ariesaema curvatum (ACL) was carried out using steady state as well as time resolved fluorescence and CD spectroscopy under various denaturing conditions. An intermediate with altered tryptophan microenvironment was detected in the phase diagram, which exibited pronounced secondary structure and hemagglutinating activity in presence of 0.25 M Gdn-HCl. An acid induced molten- globule like structure possessing activity and higher thermostability was detected. Transition to the molten globule state was reversible in nature. The lectin retained hemagglutinating activity even after incubation at 95 A degrees C. Both chemical and thermal unfolding of the lectin were found to consist of multistate processes. Fluorescence quenching of ACL was strong with acrylamide and KI. The single tryptophan was found to be surrounded by high density of the positively charged amino acid residues as shown by a ten fold higher K(sv) for KI compared to that for CsCl. The average lifetime of tryptophan fluorescence increased from 1.24 ns in the native state to 1.72 ns in the denatured state.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.107
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